28/11/2013 13:09:00

through water. As you walk through water, the water puts a force on
you and prevents you from walking through it. But now, think about walking
through honey. It's even more difficult. Honey is much more viscous than
water is. And it's much more difficult to walk through honey than is to walk
through water. Honey has a much higher viscosity.

Viscosity always involves the resistance of the fluid to flow. It's a

measure of how much resistance the fluid has to the flow. The fluid puts a
force or a stress that prevents the flow. The stress is the viscosity times the
rate of flow, or the rate at which the fluid flows over itself, the strain rate of
the fluid. Here's the formula for the viscosity. The units are stress times
time, or Pascal seconds. There are many examples that we were told about
by Nathan Myhrvold. He explained why viscosity is very important. And there
are many culinary examples. The simplest, of course, is water, which flows
much more easily than oil. Water is much less viscous than oil. But oil has a
viscosity that changes very strongly with temperature. If you increase the
temperature, the viscosity of oil decreases quite substantially. In fact, if you
heat it up enough, it can become as low viscosity as is water. Many fluids
have a very strongly temperature-dependent viscosity. And we use that in
cooking very often.

To understand viscosity from a more molecular view, let's look at this

little cartoon. The fluid is made up of many, many molecules. And the
molecules are constantly moving around. But in order to cause the fluid to
flow like this, we have to cause the molecules to move over one another. In
fact, for the fluid to actually flow, the molecules have to exchange places
with each other. And so the viscosity depends on how fast they change
places with each other. So the viscosity is given by the density times the
speed of the molecules times their size. It's just a measure of how fast the
molecules move over one another. And you can see immediately that larger
molecules take longer because they have a longer way to go to move over
one another. In fact, the speeds of the molecules are almost independent of
the different kinds of fluids.

What changes most is the size of the molecules. We can make an

estimate of what the viscosity is. The speeds of molecules are always about
the same. They're typically about 1 and 1/2 to 2 kilometers per second.
That's the speed that the molecules move past one another. The densities of
fluids are also quite similar. They're about 1000 kilograms per cubic meter,
10 to the 4 kilograms per cubic meter. So we can easily estimate what the
viscosity is of water. We just take the density times the speed times the size
of a water molecule. And for the size of a water molecule, I'll take 3
angstroms, or 3 times 10 to the minus 10 meters. If use these, I get a value
of 4 times 10 to be minus 3 Pascal seconds, or 4 millipascal seconds. In fact,
this is very close to the value that you measure for water. The measured
value of viscosity for water is about 1 millipascal second, 1 times 10 to the
minus 3 Pascal seconds.

Nathan told us that there are four ways that chefs use to control the
viscosity. There are reductions. There's starch-based thickener. There's
making an emulsion by adding fact, or using modernist thickeners, where
small amounts of material, small amounts of a polymer, are added to
increase the viscosity by large amounts. In all cases, what we're doing is
adding something to the fluid. In the case of reduction, we're reducing the
amount of liquid. And what remains are particles, or non-volatile solids. This
increases the concentration, or the concentration of the solids in the liquid.
In the case of starch, we're adding starch granules. In case of fat, or making
an emulsion, we're adding drops of fat. And the drops of fat behave just like
particles. In the case of the modernistic thickeners, we're adding polymers.
And they also have the effect of adding something to the fluid. And this is
what increases the viscosity of the fluid.

The simplest way to understand this is to think of particles in the fluid.

Imagine particles in the fluid. When the fluid flows, the particles also flow.
And they have to flow over one another in order for the whole suspension,
the whole fluid, to flow. The way they behave depends on the concentration
of the particles in the fluid. It depends on the volume of the particles, or the
volume that the particles occupy in the fluid. This is called volume fraction,
or the volume fraction of particles in the fluid. We can calculate that easily.
We calculate the volume of each of the particles. And we take the total
number of particles times their individual volume and divide that by the total
volume of the fluid. That gives us the volume fraction of the particles in the
fluid. That's the important parameter that determines how the particles
impact the viscosity of the fluid. That's the important parameter that tells
you how the particles behave when they flow, when they flow in the fluid,
and how they resist the flow, or how they add to the resistance of the flow of
the fluid.

When there are very few particles in the fluid, or their volume
fraction's very low, then they have almost no effect at all. When the fluid
flows, the particles just flow with the fluid. There's no interference of one
with another particle. The particles flow along. And they don't see their
neighbors. In that case, the viscosity of the fluid is just the viscosity of the
fluid itself. The particles play no role whatsoever. However, when the volume
fraction of the particles increases, then they become crowded. They interfere
with each other. It's more difficult for the particles to flow over one another.
And they collide with each other. They move on top of each other. They take
much more volume. And the flow is restricted. In this case, the particles
really impact the flow of the fluid and increase the viscosity of the fluid.
However, for that to happen, the volume fraction of particles has to be quite
high. It has to be sufficiently high that they can't easily flow over one
another. This doesn't happen unless the volume fraction of the particles gets
to be of the order of 50%, or half the volume of the fluid is occupied by the
particles.

When the dividing fraction is so high, then the particles can't easily
flow over one another. And this interference with the flow causes the
viscosity to increase. Now we can understand, in a very simple way, why
starch is so effective at increasing the viscosity. Remember that Nathan told
us that you change the viscosity of a fluid by adding a lot of starch. But in
his case, a lot of starch was only about 15%. Why does this happen? Well,
the starch forms granules. And the granules are dissolved in the fluid. But
two things happen when the granules are dissolved in the fluid. First, the
starch granules expand. They absorb water. And they get larger. As we show
in this little cartoon, the volume gets larger. And so the effective volume
fraction of the starch granules increases. And while you may start out with
only 15% volume fraction, when they've expanded, then they can occupy a
much larger volume fraction. So water inside the starch granules doesn't
flow. It flows with the granules themselves. And the effective volume fraction
goes up. And therefore, the viscosity goes up.

The second way that starch can increase the viscosity of the fluid is
that the granules stick together. In that case, they form these more tenuous
structures, as we show here. The volume of these tenuous structures is the
volume of the structures themselves plus all the water that they enclose, as
shown by this circle. This increases the effective volume fraction of the
particles. It allows them to occupy more volume because they pull the water
along with them. This increase in volume fraction of the particles also leads
to an increase in the viscosity of the fluid. And that's how you can greatly
increase the viscosity of a fluid, even if you don't have, essentially, 50% of
the volume. You have 50% of the volume fraction of particles because the
particles occupy a much larger effective volume.

Indeed, in all cases, in order to increase the viscosity of the fluid, you
need to increase the volume fraction of the particles, or whatever it is in the
fluid, up to about 50%, or somewhat higher. It can be larger structures of
the starch granules. It can be expanded starch granules. The same thing
happens if you do a reduction. You reduce the amount of fluid, and therefore
increase the volume fraction of whatever is left over, be it solids or solids
that are stuck together. But somehow, you're increasing the volume fraction
of the particles in the fluid. The same thing happens with an emulsion.
There, you're putting drops in the fluid. The drops have to occupy something
like 50% of the volume of the fluid in order to get an increase in the
viscosity. This can happen either by adding enough drops, or by having the
drops sticky and forming these larger, tenuous structures in exactly the
same way that the starch granules did.

Hello. It's Harold McGee again, talking with you this week about
viscosity and about sauces. Viscosity is a basic property of fluids. To a cook,
viscosity really comes down to thickness-- how easily a particular liquid
flows. And the biggest category of food preparation to which this is relevant,
really, is sauces. In sauces, we're creating preparations that contain a lot of
flavor, but that are viscous. That is to say, they flow slowly. They cling to
foods. They don't just roll right off them so that those foods end up with
more flavor on them. And in the mouth, sauces linger on the surfaces of our
time and our palate and so on, and again, help the flavor persist, help us
take a longer pleasure in the flavors of the foods. Like gelation, viscosity is
often a manifestation of long molecules in the fluid that are interfering with
the flow of the water. Usually, it's a water solution-- so long molecules
interfering with the flow of the water that they're suspended in. That's not
the only way that you can make a sauce viscous.

You can also slow the flow of the water by filling the liquid with
droplets of a second liquid to get in the way of that flow. That second liquid,
of course, has to be something that doesn't mix with the first liquid. And
that's the subject of emulsions, which we'll get to next week. This week,
though, we're focusing on polymers. And they're these long molecules that
interact with each other when they're suspended in water, dissolved in water,
and interfere with the flow of fluid around them and through them. They're
not bonded into a solid network, like a gel. They remain mostly separated
and suspended. But they get in the way of the flow of the surrounding water.
The original polymers are biopolymers.

When we talk about polymers these days, often, we're talking about
the things that make plastics. But the original polymers were and are
macromolecules that help make up our bodies and the structures of plants.
So these are, in one case, chains of sugars that make up starch and pectin
and other plant materials-- often cell wall materials, structural materials-and then chains of amino acids that make up proteins. And they're what
constitute much of our body. And the classic sauce thickeners are, in fact,
these polymers-- gelatin from meats and starch from plants. Meat sauces
are classically made by dissolving out the gelatin from meat with long
cooking. And then you end up with this fluid from the meat that's rich in
gelatin. And then you cook that down to concentrate it even further. And the
more you cook it down, the more concentrated the gelatin solution gets and
the more viscous the solution is.

In the case of starch-thickened sauces, the classic one is bchamel,

which is made simply by cooking milk and flour together-- flour containing
the starch. And that's used in lasagna and other pasta dishes and moussaka.
It's used as the base for cheese sauces. And starch, of course, is often used
to thicken soups and souffl bases. And you can think of things like pastry
creams and puddings and pie fillings as essentially think, sweet versions of
this original white sauce. Starch has some disadvantages as a thickener. It
doesn't stand up very well to freezing. And the starch chains can slowly
shorten for a variety of reasons. And when that happens, the sauces become
thinner. Starch is also susceptible to enzymes that can digest it. Those
enzymes are called amylases-- amylose-breaking enzymes. And amylases
turn out to be abundant in egg yolks.

So if you're making any kind of dish that has a combination of egg and
starch to thicken things-- for example, many pie fillings-- you have to make
sure that you cook that combination thoroughly to knock out the amylases
so that once you're done cooking, the amylases don't go to work and break
down the starch and turn the nice, thick filling into a thin liquid. And it turns
out that our saliva contains amylase. So when we put a starch-thickened
sauce in our mouse, or a spoonful of pudding, and we roll them around
before swallowing, the amylases is in our mouths actually break those
starches down and thin the consistency of the sauce as we're doing it. And if
you pay attention next time you have a spoonful of pudding, you'll notice
that thinning before you swallow. Because starch isn't the ideal thickener,
there are other sources of long molecules for thickening water-based fluids
that are more stable or otherwise more useful.

These were first developed and used in the food industry as stabilizers
of various kinds and as starch alternatives. Then later on, around the year
2000 and thereafter, they were discovered by modernist chefs and they
began to be used in restaurants. And these include gums from seeds-things like locust bean gum, also known as carob gum. There's guar gum.
There's the gum that comes out of flax seeds. There are carrageenans from
seaweeds, which are especially good for milk dishes, because they react in a
useful way with the calcium in milk. They've been known and used for a long
time in Ireland in making puddings. And then there are gums from microbes.
Gellan and xanthan gums both come from microbial fermentations.

Now, you're learning about relatively simple Newtonian behavior in

fluids, where the viscosity of the fluid doesn't change much with the
circumstances. But you're also learning about the really interesting nonNewtonian fluids whose viscosity can change drastically with the
circumstances-- for example, when the liquid is simply stirred. So some
things will get thicker when they're stirred-- when they have sheer force
applied to them. A very simple example is suspension of cornstarch. If you
take one volume of water and two volumes of cornstarch and try to mix
them together, it seems to act like a liquid as long as it's sitting there and
you're not doing anything to it, but then the moment that you try to stir it, it
sets up and turns into a solid that's impossible to move. And then there's the
reverse of that, sheer thinning, which we experience every time we try to
get ketchup out of a bottle. It's sitting there and very, very thick when it's at
rest. We try very gently to get it to move, and that gentle force doesn't
make a difference. By the time we give it enough force to get it moving,
then it liquefies and gets very, very thin. And then we end up with much
more ketchup than we want.

There's an example from haute cuisine from fine dining restaurants

that's a wonderful example of sheer thinning. It turns out, of course, if you
think about the use of sauces when you're presenting a dish, the fluidity of a
sauce is a disadvantage when you're trying to arrange the foods beautifully
on a plate, because, of course, the sauce flows. And so you put it in one
place to have it take its place in the composition of the plate. And by the
time it gets to the table, it's moved around. So what you can do-- and this is
something discovered by Heston Blumenthal in England about 10 years ago.
You can make a solid gel with agar. So you take whatever you're making the
sauce with, gel it into a solid with agar. You then take that solid gel and
throw it into a blender and blend it and break it down. And what you end up
with is a hybrid. There are still particles in there of gel, where the polymer
molecules have immobilized the water. But then in the places where the gel
has been broken, some of the liquid, some of the water, is able to flow. It's
still thickened by the polymer molecules, but it's not locked into place as it
was in the original gel.

What that means is that you have a hybrid called a fluid gel, which
behaves like a solid when there's no force applied to it, but then flows when
you do apply force. So what that means is you can paint with that sauce on
a plate and put it in a particular place and make a particular design with it.
And once you're done and you lift the spoon from the plate, the sauce stays
exactly where it was. It doesn't flow. But then when you take a spoonful of it
and put it in your mouth and you're tongue applies a sheer force to it, then it
becomes this wonderful lovely flowing sauce again. So you have the best of
both worlds. It's a wonderful example of science contributing to the progress
of the artistry of cooking.

Instructions in the recipe that help keep the temperature below the
threshold are:

Continuing whisking the mixture while in the saucepan

Removing the saucepan from the stove burner

Placing the saucepan in cold water

Suspensions mixtures of two or more substances that fail

to dissolve completely in one an- other are found in almost all

foods. In a suspension, one or more substances constitute a
dispersed phase surrounded by a continuous (usually fluid) phase.
At high volume fractions, suspensions in- crease the viscosity of
food or even lend solidity, as demonstrated by our e

quation of the week:

c
where r is the radius of the droplets, is the critical volume

c
fraction ( 0.64 for randomly- packed spheres), and is the
interfacial tension the energy required to form a given area of
inter- face (units: J/m2 or, equivalently, N/m). The interfacial
tension reflects the fact that water molecules at the phase
boundary usually cannot form as many hydrogen bonds as they
could if surrounded by other water molecules, so the formation of
the interface is unfavorable. In the absence of surfac- tants, =
72 mN/m for water-air interfaces and 24 mN/m for water-oil
interfaces.

As a result of the interfacial tension and curved boundary,

the pressure inside round droplets/bubbles is p = 2/r higher
than the pressure outside. This pressure difference, called the
Laplace pressure, makes it difficult to deform small
droplets/bubbles against one another when a stress is applied, as
conveyed by our equation of the week above.

Four ways that suspensions fail

Creaming/sedimentation: Separation of phases by gravity

due to density differences.

Coalescence: Bubbles/droplets merge on contact to decrease

interfacial energy.

Phase inversion: The dispersed phase becomes the

continuous phase, lowering .

Ostwaldripening:Despiteanenergybarrier,individulmoleculesfr

omthedispersedphaseocca
sionally dissolve in the continuous phase, through which
they can travel to other droplets/bubbles. Over time, there is a
net movement of molecules from small bubbles/droplets (where
the Laplace pressure is higher) to larger ones.

Strategies for stabilizing suspensions

Surfactants (surface active agents) decrease the rate of

coalescence and Ostwald ripening. Amphiphilic molcules (those

with both non-polar and polar regions), including lipids like lecithin
and others found in cell membranes, make excellent surfactants
at oil-water interfaces; solid par- ticles like denatured proteins can
act as surfactants at both oil-water and air-water interfaces. By
coating the surface, surfactants sterically prevent droplets and
bubbles from coalescing and hinder individual molecule
movement to/from the continuous phase. Some surfactants are
also charged, causing active repulsion between droplets/bubbles.

Increasing the viscosity hinders the movement of the

dispersed phase through the continuous phase, decreasing the

rate of emulsion failure. Changing the temperature can also
stabilize an emul- sion by altering the viscosity and the solubility
of dispersed phase molecules within the continuous phase
(potentially limiting Ostwald ripening).

Nathantoldusthattherearefourwaysthatchefsuse

tocontroltheviscosity.Therearereductions.There's
starchbasedthickener.There'smakinganemulsionbyadding
fact,orusingmodernistthickeners,wheresmallamountsof
material,smallamountsofapolymer,areaddedtoincrease
theviscositybylargeamounts.Inallcases,whatwe're
doingisaddingsomethingtothefluid.Inthecaseof
reduction,we'rereducingtheamountofliquid.Andwhat
remainsareparticles,ornonvolatilesolids.This
increasestheconcentration,ortheconcentrationofthe
solidsintheliquid.Inthecaseofstarch,we'readding
starchgranules.Incaseoffat,ormakinganemulsion,
we'readdingdropsoffat.Andthedropsoffatbehavejust
likeparticles.Inthecaseofthemodernisticthickeners,
we'readdingpolymers.Andtheyalsohavetheeffectof
addingsomethingtothefluid.Andthisiswhatincreases
theviscosityofthefluid.

Thesimplestwaytounderstandthisistothinkof

particlesinthefluid.Imagineparticlesinthefluid.When
thefluidflows,theparticlesalsoflow.Andtheyhaveto
flowoveroneanotherinorderforthewholesuspension,the
wholefluid,toflow.Thewaytheybehavedependsonthe
concentrationoftheparticlesinthefluid.Itdependson
thevolumeoftheparticles,orthevolumethatthe
particlesoccupyinthefluid.Thisiscalledvolume
fraction,orthevolumefractionofparticlesinthefluid.
Wecancalculatethateasily.Wecalculatethevolumeof
eachoftheparticles.Andwetakethetotalnumberof
particlestimestheirindividualvolumeanddividethatby
thetotalvolumeofthefluid.Thatgivesusthevolume
fractionoftheparticlesinthefluid.That'stheimportant
parameterthatdetermineshowtheparticlesimpactthe
viscosityofthefluid.That'stheimportantparameterthat
tellsyouhowtheparticlesbehavewhentheyflow,whenthey
flowinthefluid,andhowtheyresisttheflow,orhowthey
addtotheresistanceoftheflowofthefluid.

Whenthereareveryfewparticlesinthefluid,or

theirvolumefraction'sverylow,thentheyhavealmostno
effectatall.Whenthefluidflows,theparticlesjustflow
withthefluid.There'snointerferenceofonewithanother
particle.Theparticlesflowalong.Andtheydon'tseetheir
neighbors.Inthatcase,theviscosityofthefluidisjust
theviscosityofthefluiditself.Theparticlesplayno
rolewhatsoever.However,whenthevolumefractionofthe
particlesincreases,thentheybecomecrowded.They
interferewitheachother.It'smoredifficultforthe
particlestoflowoveroneanother.Andtheycollidewith
eachother.Theymoveontopofeachother.Theytakemuch
morevolume.Andtheflowisrestricted.Inthiscase,the
particlesreallyimpacttheflowofthefluidandincrease
theviscosityofthefluid.However,forthattohappen,the
volumefractionofparticleshastobequitehigh.Ithasto
besufficientlyhighthattheycan'teasilyflowoverone
another.Thisdoesn'thappenunlessthevolumefractionof
theparticlesgetstobeoftheorderof50%,orhalfthe
volumeofthefluidisoccupiedbytheparticles.

Whenthedividingfractionissohigh,thenthe

particlescan'teasilyflowoveroneanother.Andthis
interferencewiththeflowcausestheviscositytoincrease.
Nowwecanunderstand,inaverysimpleway,whystarchis
soeffectiveatincreasingtheviscosity.Rememberthat
Nathantoldusthatyouchangetheviscosityofafluidby
addingalotofstarch.Butinhiscase,alotofstarchwas
onlyabout15%.Whydoesthishappen?Well,thestarchforms
granules.Andthegranulesaredissolvedinthefluid.But
twothingshappenwhenthegranulesaredissolvedinthe
fluid.First,thestarchgranulesexpand.Theyabsorbwater.
Andtheygetlarger.Asweshowinthislittlecartoon,the
volumegetslarger.Andsotheeffectivevolumefractionof
thestarchgranulesincreases.Andwhileyoumaystartout
withonly15%volumefraction,whenthey'veexpanded,then
theycanoccupyamuchlargervolumefraction.Sowater
insidethestarchgranulesdoesn'tflow.Itflowswiththe
granulesthemselves.Andtheeffectivevolumefractiongoes
up.Andtherefore,theviscositygoesup.

Thesecondwaythatstarchcanincreasetheviscosity

ofthefluidisthatthegranulessticktogether.Inthat
case,theyformthesemoretenuousstructures,asweshow
here.Thevolumeofthesetenuousstructuresisthevolume
ofthestructuresthemselvesplusallthewaterthatthey
enclose,asshownbythiscircle.Thisincreasesthe
effectivevolumefractionoftheparticles.Itallowsthem
tooccupymorevolumebecausetheypullthewateralongwith
them.Thisincreaseinvolumefractionoftheparticlesalso
leadstoanincreaseintheviscosityofthefluid.And
that'showyoucangreatlyincreasetheviscosityofa
fluid,evenifyoudon'thave,essentially,50%ofthe
volume.Youhave50%ofthevolumefractionofparticles
becausetheparticlesoccupyamuchlargereffectivevolume.

Indeed,inallcases,inordertoincreasethe

viscosityofthefluid,youneedtoincreasethevolume
fractionoftheparticles,orwhateveritisinthefluid,
uptoabout50%,orsomewhathigher.Itcanbelarger
structuresofthestarchgranules.Itcanbeexpandedstarch
granules.Thesamethinghappensifyoudoareduction.You
reducetheamountoffluid,andthereforeincreasethe
volumefractionofwhateverisleftover,beitsolidsor
solidsthatarestucktogether.Butsomehow,you're
increasingthevolumefractionoftheparticlesinthe
fluid.Thesamethinghappenswithanemulsion.There,
you'reputtingdropsinthefluid.Thedropshavetooccupy
somethinglike50%ofthevolumeofthefluidinorderto
getanincreaseintheviscosity.Thiscanhappeneitherby
addingenoughdrops,orbyhavingthedropsstickyand
formingtheselarger,tenuousstructuresinexactlythesame
waythatthestarchgranulesdid.

28/11/2013 13:09:00

This week we're going to study the physics of baking. Baking has
arisen already on several occasions in this course. During the first week I
told you about my favorite recipe Nestle Toll House chocolate chip cookies.
And we discussed the number of molecules there were of the different
ingredients. A couple of weeks ago you made what is at least my favorite
lab in this course-- the molten chocolate cake which of course involves the
physics of baking. But so far we haven't been able to actually go into the
physics of baking-- that is how do recipes for baked goods work and
produce the delicious outcomes that we all so much enjoy. And the reason
for that the reason that we haven't discussed baking as of yet is that as
you will see this week the physics of baking involves many--in fact, if not
most--of the ideas that we've discussed up until this point.

Baking involves elasticity viscosity emulsions heat transfer solubility

many concepts like that. And this week we're going to go through what is
going to be on one hand a bit of a review of the concepts that we've
discussed up until this point. And the other hand we're going to show you
how these ideas apply to baking. So before we begin I just want to give one
caveat. We are not professional bakers. We are scientists. And our intent in
this week's baking discussion is not to basically go through every method
and every technique that is required to basically make a baked good
delicious. What we're going to do is to expose the basic scientific issues that
underlie baking. And by putting them together in your own mind they will
hopefully help you make sense of recipes. Before we begin, I want to quickly
go through and just discuss how baking involves many of the physical ideas
we've discussed to date.

Let's start with elasticity. You will remember in week four of the course
Bill Yosses made this wonderful strudel dough in which he showed you how
stretchy and elastic strudel dough was. And indeed the elastic properties of
dough are one of the central features of baking. What gives rise to that
elasticity? Well, there are at least three different things that give rise to the
elasticity of baked goods if not more. The three that I want to emphasize
though and are probably the most important are first the properties of
gluten. Pia talked earlier about glutenin molecules and their interactions and
how they give rise to the elasticity of strudel dough. Secondly, the elastic
network that occurs in eggs-- many baked goods involved eggs. And you all
know from simply cooking eggs that you produce a scrambled egg or a
whatever kind of egg, which actually has an elastic modulus. And the same
types of networks of gelation networks that occur in eggs also occur in
baked goods, presumably that include eggs.

And the third main ingredient of elasticity is that given by starches and
sugars, which are present in both flour and also any added sugar. So for
starches especially, you might recall from last week's discussion of viscosity
that when you pour starch granules into a liquid and you then heat up the
liquid the starch granules expand. And Dave explained to you how when the
starch granules expand that they interact with each other. And in principle,
they get to the point where there are so many starch granules that when
you squish on the bread or whatever the dough is that has the starch
granules in it that also creates an elastic modulus.

So when you think about what is giving rise to the elasticity of baked
goods, it's really very complicated. It involves the interplay of all three of
them in whatever configuration happens to be made when you go through
your baking protocol. But these are all wonderful illustrations of elasticity. A
second major idea that underlies baking is viscosity. You might say how
could it include viscosity because after all when you take a cake out of the
oven you can squish on it and it's got an elastic modulus? You can put a
weight on it and measure its elastic modulus. Maybe when you measure the
elastic modulus for the food in elasticity week of the course, you used a
baked good.

But you see baked goods also have viscous properties. And the reason
for that is that if they didn't breads wouldn't rise cakes wouldn't expand
cookies wouldn't expand when you make them in the oven. Any time
something expands and rises that involves the flowing of molecules by each
other. And it's indeed this viscous property of batters that is absolutely
critical for their success. A third scientific idea that is important in baking is
emulsions. So cakes our emulsions. To see that what you can do is just cut
open a cake and look inside at the structure. And what you see are lots of
little bubbles. Those bubbles of course are the result of gas expansion that
occurs during baking. And that is something that we will also talk about.

But the fact is that cakes and baked goods tend to be made of bubbles
that are packed together. So for this reason the ideas that we discussed in
emulsions week are also going to be important. And indeed you will recall
then that we said that when the volume fraction of bubbles reaches some
critical amount then they start to squish into each other and things stop.
And that same sort of process occurs during baking. Another scientific idea
that is important in baking is heat transfer. You after all heated a molten
chocolate cake. And by cooking it you were able to measure the heat
diffusion constant of water. For that, our wonderful equation L is equal to the
square root of 4Dt came in handy.

And that's what we used indeed to make the measurement. The heat
transfer to baked goods obeys the laws of diffusion. But there's an additional
complication, which is that cakes rise, baked goods rise. And when they rise
heat actually is able to move not just by undergoing random walks but
actually moves because of the rising itself. And this can change depending
on the circumstance the law that governs heat transfer in a baked good
which makes it more complicated than those that we discussed before.

Finally, a last set of scientific ideas that are important in baking involve
chemical reactions producing gases which we discussed early on in this
course and also the general idea of solubility. After all when you make a
cake and you put sugar in it there's always water and there's sugar. And
the sugar dissolves in the water. And that's actually important for the entire
baking process. So the ideas that we've talked about solubility and the
dependence of solubility on temperature all come into play.

So as you can see the physics of baking involves many of the

scientific ideas that we've discussed so far in this course. And that is indeed
why we haven't been able to delve into it before. So now let's dive in and
start to explore how these different physical processes interplay with each
other to make delicious baked goods. And to help us with this we're very
fortunate to be able to visit the kitchen of Joanne Chang of Flour Bakery
who's going to show us how to make yellow birthday cake how to make pie
dough and how to make bread. And you will see when you watch her go
through and describe all of the different thing she's thinking about when she
makes these products how these different physical elements come into play.

Now we turn to a discussion of the elasticity of baked goods. The

elasticity of baked goods comes from two things the proteins that are in the
baked goods which make protein networks that contribute to the elasticity,
number one. And number two, the starches that are in the baked goods
starches being the starch granules from flour or any added sugar which can
tend to pack together and also cause elasticity cause the material to have
an elastic modulus. So if you cut open a baked good what you see, of
course, are lots of air bubbles. And the air bubbles, in principle themselves,
can also contribute to the elasticity in a way that we described last week
when we discussed emulsions. But around the air bubbles are these layers of
material which are made of the proteins and the starches. And those are, if
you simply go and make a measurement, tend to be the dominant feature of
the elasticity of baked goods. So we're going to focus on these.

Now, the situation is actually really very complicated for figuring out
what is going on. It's much more complicated than the simple days when we
were telling you about the elasticity of an alginate gel. There we put up
these straightforward pictures where we had polymers. We had cross-links.
And we said. oh look isn't it great? e is equal to u over l cubed, where e the
elastic modulus and all that matters is the cross-link distance. Here, it's
more complicated because we have several things that are acting in parallel
to create the elasticity of the baked good. There are the networks from the
glutenin. There's the networks from the eggs. There's the starch granules.
And they're organized in some fashion which is very hard to know in detail
that basically are contributing to the elasticity.

The way that the organization occurs almost certainly depends on the
cooking process that you use. It depends on as we will discuss in a little bit,
whether you've added fat or salt or something else to the batters. It
depends on the pH of the batter. It really is a very complicated beast. And
there's no chance that we're going to be able to dive into this in great detail.
Mainly because we simply just don't understand it very well. So instead what
we're going to do is something very simple which at least we think is
somewhat illustrative of what is going on. Which is that we're going to
consider the batters for a variety of different baked goods. And we're going
to simply count the number of molecules of different types that are in the
batters in a given volume of batter. From that we'll see how far apart these
molecules are likely to be. And we can start to put together a mental picture
of under what conditions are one network forming rather than the other?
When might egg be important? When might glutenin be important? When
might starch be important? Just things like this. And it just helps us form a
mental picture. So what I want to now do is turn to a consideration of that.

OK, so in order to delve into this we need to know what the basic
composition is of different types of baked goods pancakes versus cakes
versus breads. So you can, of course, open a cookbook. And there are rules
of thumb that are given for the different percentages that are in the different
food. So for example people often say that bread is 60% flour. But, of
course, if you've ever gone into your kitchen and followed recipes you'll
notice that it's really very highly variable how much flour you might use
how much sugar you might use how much water you might use. And even
in a recipe for a particular type. Even if you were just to focus on cookies. So
in order to get some view of the range of ingredients that basically
contribute to a particular type of baked good we decided to do something a
bit peculiar, namely, the following.

So with the help of two wonderful computer science students Elaine

Angelino and Diana Cai we basically decided to go on the web and to look at
what the components were in as many different types of each baked good as
possible and to somehow visualize the space of possible ingredients that can
be used in the different components. And I want to just take a moment to
tell you about this because this will sort of inform how much of each
component tends to be in a given type of baked good so we can think about
this question of elasticity and physical properties in more detail. OK, so to
show you how we're going to do this, I want to just start out with bread. So
here's a typical recipe for bread. And as I said before it contains 60% flour
and 40% water.

So what I want to do now is to represent this on a plot. So here's a

plot. And on the y-axis the plot contains the water content of bread. And on
the x-axis it contains flour content. And since the flour is 60% and the
water is 40% I can represent this particular bread recipe as a dot on this
diagram. That's this particular bread recipe. Now you, of course, might make
a different bread recipe. And if you do that then your recipe might be a
different dot on the diagram. So this same method can be used in more
complex recipes. For example, this recipe for bakers best brownies, which is
actually my favorite brownie recipe and also is one of the first brownie
recipes that was ever created. Now those of you who bake brownies a lot
know that you don't actually tend to add water to a brownie recipe. So there
is water in the recipe, of course, which comes from the eggs, the ingredient
of the eggs which contains a substantial amount of water.

But in brownies, there's much more sugar than there is flour. That was
the main idea that underlies brownies. And so the amount of sugar in this
recipe is about 41%. And the amount of flour is about 12%. So if I want to
represent this on a plot then a good way to do it is to plot on the y-axis the
sugar percentage on the x-axis the flour percentage. And on this plot, the
baker's best brownie recipe is here. It's just a dot, which I'm going to put as
a star because I like this recipe right in the middle of this plot. Now I'm
going to refer to, in what follows, this type of diagram where we plot the
percentage of one ingredient on one axis and the percentage of the other
ingredient on the other axis as a bakery phase diagram. This is perhaps an
abusive notation of the word phase diagram. But it makes me happy. And it's
sort of describes what we're trying to do.

So now here's the deal. So let's just focus on brownies first. So you all
know that some of you like one brownie recipe. Some of you like another.
And you know that if you look at different recipes if you just go to the web
or you open up a cookbook and you look at different recipes the
percentages of sugar and flour are going to change around. Some of them
will have 40% sugar. Some of them are going to have 35% sugar. And it will
change around. So we wanted to get some idea of what is the region in this
plot of flour versus sugar that corresponds to brownie recipes. I mean, we
know the brownies have lots of sugar in them. And so we know that
brownies should occur in a region where there's more sugar than flour,
because otherwise you wouldn't call it a brownie. You might call it a cookie,
for example. But the question is how does the data look?

So what we did with Elaine and Diana was to basically go to the web
and to download as many recipes as we could. So computer scientists have
these wonderful methods that basically can go to web pages. And if you
know how to read them can literally what they call scrape them and scrape
off the recipes. And then you can basically take all of the recipes that you
found and arrange them in an Excel spreadsheet that looks like this. So this
Excel spreadsheet has many recipes in the different rows. And has many
ingredients in the columns because, of course, there's a huge number of
ingredients that there are. But what we then did was to simply focus on flour
and sugar. And for all of the brownie recipes we put a dot every time in this
diagram of sugar as a function of flour to show where all the recipes lie. And
here is the answer.

So each one of these purple dots corresponds to a brownie recipe. The

star is the baker's best brownie recipe. And this purple region is essentially
the region of dots which contain the brownie recipes within them. And so
what you see is that if you make something which is a brownie we basically
expect it to be in this general region. So that's brownies. And, of course, the
reason that this is interesting is because you can go and look at different
types of recipes for this. So let's consider now cookies. So if we compare the
baker's best brownie recipe to a sugar cookie recipe as I show here the
ingredient list is really quite different. The sugar cookie recipe despite the
word sugar in the title actually has less sugar than the brownies do. But we
can, of course, take this sugar cookie recipe and in the same way represent
our sugar cookie recipe on our plot.

So here what I've done is I am going to show you essentially all sugar
cookie recipes that we downloaded from the web and compare them with the
brownie recipe. So the purple dots correspond to the brownie recipes. The
blue dots correspond to the sugar cookie recipes. And as expected the two
separate. When we give brownies a name it's because they have a different
set of ingredients then a cookie. And we all basically tend to agree on this.
Chefs tend to agree on what the different words mean. And indeed sugar
cookies contain less sugar. And, of course, we can continue this. We can go
and look for pancake recipes. Pancake recipes, you know, have very little
sugar. Some pancake recipes have sugar. They have some amount of flour
which it turns out if you look at this plot is between the amount of flower for
brownies and cookies. So the yellow dots are the pancake recipes. And they
tend to have very little sugar. And then we can just sort of go crazy and keep
putting on more different types of baked goods.

So this last plot shows cakes and breads and pancakes and cookies
and brownies. And each color corresponds to a different type of baked good.
So for example the red crosses correspond to bread loaves. And you will
see they also have less sugar in them than the brownies or even the cookies.
But tend to have more flour. The flour percentage in breads is more like 60%
as we saw. Although there's actually a fairly wide range of the bread recipes
that we found on the internet. Namely the percentage of flour and bread
tends to go between 50% and 75% or so. So there's really a very wide
range. But this shows you the different percentages that occur of ingredients
in different baked goods. Before we go on to use the conclusions from these
plots to think about the physics of baking

I just want to make one comment. So I've just spent a lot of time
plotting sugar against flour. And indeed sugar and flower are important
ingredients in baked goods. But you all know that baked goods contain many
many more ingredients that are important than sugar and flour. There's
eggs. There's liquid. There's baking soda and baking powder and so on and
so forth. And all of these things are important. So if we want to be able to
visualize this what we would have to do is to take the spreadsheets that we
have. And here again is the example of a spreadsheet with all of the recipes
as the rows and all of the ingredients as the column and somehow find a
way to visualize this in a high-dimensional space. So you could imagine
doing it in three dimensions. You could plot sugar, flour, and liquid content.
And then we could plot our dots in three-dimensional space. But the human
brain is not good at going beyond three-dimensional visualizations. So that's
pretty much the limit to what we can do.

There is however a way of visualizing these ingredients in four

dimensions which is to basically print them all out on the faces a
tetrahedron. If you do this, you can look at the variation at the same time of
flour liquid sugar and egg which at least in my mind are four of the most
important structural ingredients for baked goods and are at least the ones
that are at play here in our present discussion of elasticity. And here is
actually a representation of all of the recipes that we collected on the
surfaces of a tetrahedron that Elaine made. And you can sort of sit and stare
at it. What we're going to do actually is provide you a link to a newspaper
article which has a drawing of this tetrahedron that if you print it out on
paper you can cut it out. And you can stare at the ways that different baked
goods fill up ingredient space yourself. And contemplate why they're all so
different.

So you would just watched Joanne Chang make a delicious, fluffy,

tender, yellow birthday cake. And as she walked through the cake with us
she kept stressing the different ingredients and how they contributed to the
fluffiness of the cake. So let's look at one of them-- baking soda. So, baking
soda as Joanne told us is a basic ingredient. It has a pH that is higher than
7. And so it reacts with some of the acids in the recipe. So, for example, the
buttermilk in the case of the yellow birthday cake is what reacts with the
baking soda. So let's look more closely at this reaction. I think you've
probably all at some point experienced in your lives mixing baking soda
with vinegar. Vinegar is an acid (the video erroneously states that it is a
base). And there are various ways you can experiment with this mixing and
this chemical reaction.

One way would be to just add them together. And the gas that is
produced, which is carbon dioxide would just expand so quickly that you
could even explode things. So let's look more closely at this. In this reaction,
we have baking soda and we have vinegar. And it produces a gas-- carbon
dioxide. Here is the boring way to do this or the somewhat scientific way to
do this. If we actually wanted to know how much gas is produced in this
reaction what we could do is we could mix the two ingredients. And we
could measure the gas. So how would we measure the gas?

Well, so here's a demo set up with three different Erlenmeyer flasks.

And they all have different amounts of baking soda in the bottom. And the
vinegar is up here in top in the balloon. And so, as we flip the balloon the
two reagents are going to react. And there's going to be gas produced. And
we can the estimate the gas produced by estimating that the balloon is a
sphere. We can plug the radius of the sphere which in this case is
approximately maybe 5 centimeters and 10 centimeters and we can plug it
into the volume for a sphere and find out approximately how much gas is
produced. Now, this is somewhat an approximation, as is often the case in
this class, because, as you can imagine, there's also more pressure in the
balloon. And so there's probably a little bit more gas in there than it looks
like from this. This is actually the reaction that contributes to the fluffiness of
the cake. This is the very same reaction.

So, let's look more closely at this. So baking soda is sodium

bicarbonate. And vinegar is acetic acid. And they combine to produce carbon
dioxide which is a gas. And it turns out they also produce water and sodium
acetate. And so we now need to of course balance this reaction. And we
see that one mole of baking soda corresponds to one mole of carbon dioxide.
And so let's look at this Erlenmeyer flask in particular. So this flask has 5
grams of baking soda. And so if we go through the calculation, we see that
that's 0.06 moles of baking soda which then corresponds 0.06 moles of
carbon dioxide. And we also know from before that one mole of gas is 22.4
liters in volume. And this corresponds to 1.3 liters of carbon dioxide. And
this is probably about right. If you look at the balloon, this is probably
somewhere in the proximity of a liter. So theory now corresponds with our
experiment, which is a good thing.

So let's go back now to Joanne's recipe for yellow birthday cake. So we

see here, here's all the ingredients. And we see that we use one teaspoon of
baking soda and half a teaspoon of baking powder. And baking powder, as
Joanne told us, is a mix of baking soda and an acid. And it's usually cream of
tartar. So now we want to calculate how much gas we get from the baking
powder. And baking powder is a mix of cream a tartar and baking soda. And
so that they will react perfectly, they are stoichiometrically balanced. So we
have the same number of moles of each. So if you then take their weights
into account, what this ends up being, because the weight of the cream of
tartar is higher, we have one third of the baking powder is baking soda, and
the rest is cream of tartar.

So this means that in our recipe we have one teaspoon of baking

powder. And this then gives us that we have a third of a teaspoon of baking
soda. So this is what's going to be contributing to the gas. So that's why
we're interested in this number. So we have one third from the baking
powder. And then we have a half of a teaspoon from the baking soda
already, which is what you see in the recipe. So these end up to 5/6
teaspoons. And if one teaspoon weighs five grams, then this means that we
approximately, have four grams of baking soda. Since the molecular weight
of baking soda is 84 grams per mole, this now means that we can divide four
grams over 84 grams per mole to get how many moles we have, and this is
0.05 moles. So this is how many moles of baking soda we have. And we also
know that we're going to have the same number of moles of carbon dioxide
in the end as we have of baking soda. So we also know that we're going to
end up with 0.05, moles of carbon dioxide. Now, one mole of the gas
occupies a volume of 22.4 liters. Which is a pretty big volume. So if we have
0.05 moles of carbon dioxide, this means that we have 0.05, moles times
22.4 liters per mole. And this is one liter. So at the end of all this when all
the baking soda and baking powder have reacted, we're going to end up with
one liter of carbon dioxide. And we have calculated that the initial amount of
batter is about two liters. And so according to this when we put the cake in
the oven and the gas is produced we should get about three liters total. So
there should be increase of cake of about 50%, which actually corresponds
to what Joanne got. However, we have to remember what Joanne kept
pointing out to us throughout the recipe which is that gas is also coming
from other places. And so the fluffiness of the cake is not only due to the
baking soda and the baking powder. So, for example, as you cream the
butter and the sugar, the sugar is digging out little air pockets in the butter.
And these air pockets then expand when the steam expands during the
baking. And then there's also water in general in the recipe, which expands
as we bake the cake.

Where does all this gas go? What do gasses do when you just leave
them alone? They tend to just dissipate and sort of fill whatever space they
can. And so you can imagine that the batter would probably not be able to
hold in all of the gas the way the balloons did for example. And so some of
the gas probably dissipated in the room. And in some batters, when you
make pancake batter for example you can actually see this as the gas kind
of plops up on the surface. And so you can imagine then that depending on
which batter you're using or which dough you're using so if you're baking
bread for example you can imagine that the gluten network is strong
enough to hold maybe more gas than a batter would that would more easily
dissipate the gas. So this is where all the gas goes. But as you can see, the
cake still turned out perfectly fluffy and delicious and tender.

In the previous segment, we assumed that the baking soda reacted

with the acid in the buttermilk. And so in this recipe, it was the buttermilk
that was providing the acid that contributed to the gas production. And other
common acidic reagents in recipes are things like chocolate, molasses, sour
cream. And they all have slightly different pH's. And so sometimes people
have lemon juice in recipes and the pH of that is about two. The pH of
molasses is a little over five. The pH of buttermilk and sour cream is about
4.5. And if you were to add chocolate or coffee to your recipe, they would
also be acidic. And the pH of coffee is about six. And the pH of chocolate is
around five or six, or so. And so all of these would be contributing in acid to
the baking soda and would contribute to the gas production.

So the acid in buttermilk that is reacting with the baking soda is lactic
acid. And this is also the acid that is contributing the acid in sour cream or in
other dairy products that you may be cooking with. And so depending on
which reagent you're using, is going to depend on which acid is in that
reagent. And so in coffee or in chocolate there's going to be other acids that
are basically donating their protons that are reacting with the baking soda
and contributing to the carbon dioxide production. The rate of this reaction is
still going to depend on how easily this proton has given up, which of course
we already know as the pH of the reaction. So the rate is going to depend on
the pH. And we're not going to go into that further here. But you can
imagine actually studying this by basically doing our balloon experiment and
seeing how much gas would be produced at different temperatures. And as
you're increasing the amount of acids and sort of limiting the amount of acid
you have, and see how much gas you produce. This is also what's
determining the action of double acting baking powders.

So if you've been watching this and heard us talk about how baking
powder is a mix of baking soda and cream a tartar, you may have gone to
your cabinets and actually looked at your cans of baking powder. And seen
that there isn't always just cream of tartar in baking powder. There's also
other reagents such as you may have seen calcium phosphate, or sodium
aluminum sulfate. And these are other acids and they act by affecting the
rate at which the protons are released. And so many of these acids will
release some protons at room temperature. And so some gas will be
produced here. But then as you heat the cookie or the dough, you will get a
further release of protons that will be reacting with a baking soda, and will
produce more gas. So here is a table showing a lot of common acids that
you may see on your cans of baking powder. And you can see here that
there's quite a difference in how much carbon dioxide is being released at
room temperature and when heated. And so you can imagine that perfectly
matching these acids so that you get the perfect amount of gas being
released at room temperature and then further gas released when heated,
you would get the perfectly fluffy cake or cookie.

So now that we have some idea of what the different percentages of

the, different ingredients are in different types of baked goods, I want to
now take this information and go back and think a little bit about the
elasticity, what contributes to the elasticity of different types of dough. So
let's just start with the molecule glutenin. So Pia explained to you all
already, after Bill Yosses' wonderful strudel the physics of how glutenin
molecules get together and contribute to the, elasticity of dough. And what I
want to do, actually, is just count, in a given amount of batter, how many
glutenin molecules there are so we can think about, whether or not they can
stick together and actually form a very, very tight dough as one expects to
form during baking. And we want to think about how the distances between
the glutenin molecules changes in the different types of baked good. So, to
start with, glutenin is a molecule which is about 15 nanometers long and
about two nanometers wide. It's a rod-shaped molecule.

So where does glutenin come from? Glutenin, of course, comes from

flour, and flour, of course, comes from the seeds of wheat. Now wheat seeds
have three different parts.There's the husk of the seed, there's the embryo,
which is the part of the seed that will actually grow into a plant if it's allowed
to, and there's, the part that people call the endosperm, which is essentially
the nutrient pool that basically feeds the embryo when it's allowed to grow
into a plant. So if you take 100 grams of wheat seeds, then this is actually a
table that shows the compositions of both the seed itself and the
endosperm.It turns out that all-purpose flour, which is what I'm going to
consider, here for this discussion, comes essentially from the endosperm.
And so we can see that out of 100 grams of endosperm or all-purpose
flower, there are about 10 grams of protein and 76 grams of
carbohydrates,or it's mainly carbohydrates.Those, of course, are the starch
granules, the protein is the part that contain the glutenin. So indeed it turns
out that 60% percent, and these are rough numbers, but about 60% of the
protein content of flower actually,corresponds to glutenin.

And so now, actually, what we want to do is, given an amount of

flower that a recipe calls for we would like to compute the number of
molecules of glutenin there are. Now we already showed you in the first
week of the course the dangers of weighing flour. Flour weights are
notoriously inaccurate, and we told you that that was because flour is
actually a powder, and powders pack differently.So converting from volume
to mass when you're dealing with something like a flour is a bit dangerous.
But we're just trying to get rules of thumb, here, numbers, and so
we're,going to do it anyway.And I'm going to take, let me see with my trusty
calculation, I'm going to basically say that 100 grams of flower has a volume
about 170 milliliters which corresponds to a density of about 0.6 grams per
cubic centimeter. And that's a ballpark number for the density of flour.

So if we want to compute the mass of glutenin that there is in a flower

what we have to do is take the volume of flower that we have, multiply it by
the density, 0.6 grams per cubic centimeter.We then multiply them by the
percent of the flour weight which is protein,which as I told you for allpurpose flour is about 10%.And then we have to multiply by 60% which is
the fraction of the protein mass which is glutenin. And given that, we
actually have this nice little handy formula for the,amount of glutenin that
there is given an amount of flour, and it turns out it's about 6% of the
weight is actually glutenin. Given the mass of glutenin, we can calculate the
number of molecules.We simply take the molecular weight of glutenin, which
is 75,000 grams per mole. And we take the weight, we divide by 75,000
grams per mole, and we multiply by Avogadro's number 6.022 times 10 to
the 23. And that gives us the number of glutenin molecules that we have.

So now what really matters to us is not the number of molecules that

we have, but how much distance are they apart. And we can do that by
calculating how much volume does each glutenin molecule occupy. So if we
take the total volume of batter, v, whatever that volume is, so this is volume
of batter now. It's not the volume of flour because we're going to actually
mix everything together that we have to make the batter. If we take the
total volume of batter and we divide by the number of,molecules, that tells
you how much space each molecule has. And if we then imagine that space
as being a cube, the same distance on each side, let me just call that
distance l sub g for the length between glutenin molecules, that basically
tells us how far there is between glutenin molecules.

So this is all a bunch of calculations, but now what we really want to

do is start to apply it to the different percentages of gluten that there are in
the different recipes, and let's see how far apart they are. And before I do
this, how far do you think they are apart? So let's apply this and see how far
apart the glutenin molecules are. So if we go back to this wonderful plot that
we showed you of this sugar,as a function of flour for the different recipes, if
you read it off what you see, roughly, is that pancakes are about 40% flour,
bread is about 60% flower, and cakes is about 30% flour. There's of course a
wide range, and one thing you might worry about is how different the
glutenin networks are over this range. This is something we're going to see
in a minute.

But let's just, for the sake of argument right now, compare pancakes
to bread to cakes, because we all know from our experience how different
their textures are.So what I want to do is consider one kilogram of batter. So
that's, of course, a lot of batter, but just to have round numbers, let's
consider a kilogram of batter.That's about a liter. It's actually a little less
than a liter because batter is a little more,dense than water, but we're just
trying to get rough numbers here. And so it's about a liter of batter. And so
under those circumstances, the mass of flour in pancakes would be about
400 grams, in bread would be about 600 grams, and in cakes would be
about 300 grams. So applying our rule of thumb, in order to get the mass of
glutenin, we have to multiply those numbers by 6%. So 6%, by 0.06. So
that means just calculating a little. Let's see, for pancakes, if I multiply 400
by 0.06, that gives me 24 grams. For bread, 600 by 0.06, that gives me 36
grams. And for cake, that gives me 18 grams.So that's how much glutenin
there is in each of these ingredients.

And If we now apply the formula for the number of molecules using
the molecular weight and Avogadro's number, what we find is the following.
In one kilogram of batter, there are 1.9 times 10 to the 20 glutenin
molecules in pancake batter.In bread, there are 2.9 times 10 to the 20. And
in cake, there's 1.5 times 10 to the 20. So big numbers, 10 to the
20.They're about the same, though. I mean, right? I mean, bread, I mean
for all this talk of gluten in bread, I mean there's twice as much gluten in
molecules and bread than there is in pancakes. So numbers like 10 to the 20
are hard to think about, so what we're going to,do instead, as I said before,
is to convert this to a volume.That is, how much volume does each glutenin
molecule occupy?,So we have a liter of batter, remember, and a liter is 1,000
cubic centimeters. So it's slightly more convenient to express our volume in
cubic nanometers because it's going to turn out, this shouldn't be a surprise
to you, that the distance between the molecules is measured in nanometers.

So let's see, we have to convert 1,000 cubic centimeters to cubic

nanometers.So each cubic centimeter has in it 10 to the 7 nanometers. So
that means that 1,000 cubic centimeters corresponds to 1,000 times,10 to
the 21 cubic nanometers.So that means that a liter is 10 to the 24 cubic
nanometers. So that is the volume of the batter that we have, 10 to the 24
cubic,nanometers.And now we just want to divide that by the number of
molecules that we have to find out how much space there is for each
molecule. And let me use my trusty iPad to do this calculation, and let's see
what the numbers turn out to be. So for pancakes, what we're going to do is
divide this 10 to the 24 number,by 1.9 times 10 to the 20, and that tells us
that for every molecule there's 5,263 cubic nanometers. For bread, it
corresponds to 3,448 cubic nanometers. And for cake, it corresponds to
6,896 cubic nanometers. So there's a bigger volume for the glutenin
molecules in cake then there is in bread, as you would sort of expect.

But now to sort of make this into a real number that we can think
about let's take our volume for each one and let's actually imagine that
that,volume is a cube which has the same distance on each side. I'm going
to call that l sub g for the length scale of gluten. And so I'm just going to
take that volume and set it equal to l cubed, l sub g cubed, which is the
volume of the cube, and let's ask how big the size of the cube are. So it
turns out that for pancakes, the cube is 17 nanometers big, in bread,it's 15
nanometers, and in cake its 19 nanometers.So that means that the glutenin
molecules in pancakes are about 17 nanometers apart, and in bread, where
gluten is so much stronger. It's 15 nanometers.That's a pretty small
difference between these different recipes.

So it must be that the textures of these different recipes comes from

something more than just the distance that the glutenin molecules are apart.
Now one other comment, though, about these numbers.The fact that these
numbers are small is very important, because remember I told you at the
beginning that glutenin molecules were 15 nanometers long. And we need
the glutenin molecules to cross link to basically create this elastic network
that provides the elasticity of the bread or the cake or,the pancake. With
very long molecules that are 15 nanometers long that are separated 15 to
20 nanometers apart, you can clearly form a cross link network. And that is
very important because that shows us that the glutenin, it is at least
conceptually possible, given the amount of glutenin that's in the recipe, that
it can provide the elastic backbone, and indeed it does.

Now one of the reasons that the different recipes have such different
textures even though the glutenin molecules are about the same distance
apart is that one can actually modulate the interactions between glutenin
molecules. So you'll remember our formula for the elastic modulus-- E is
equal to U over L cubed. So what we've just talked about is L-- that is the
cross-link distance. I mean the distance between the glutenin molecules
isn't the same as the cross-link distance. But it's got to be somewhere in
that range. But the other way of course to change the elastic modulus is to
change U.

And when you're baking there are several ways of doing that which I
now want to just go through and remind you of. So one is is that if you coat
the glutenin molecules with fat with something that's actually hydrophobic
you can weaken the interactions between the glutenin molecules. And that's
because the fat will coat the hydrophobic residues in the stressed out
glutenin molecule and cause the interactions between to glutenin modules to
be weaker than they otherwise would be. So oftentimes when a recipe has
butter or shortening or some other type of fat that fat is going to end up
depending exactly on the preparation of the recipe coating the glutenin
molecules. And that actually has the feature that it will weaken the elastic
network of the glutenin. And that's certainly true in cakes, right? I mean,
the reason that cakes are so much more tender in part than breads is
because of the fat content that in the cake.

So another way actually that you can modulate the strength of

interactions between glutenin molecules is to change the pH. This shouldn't
be a surprise to you. We've talked about the role of pH in modulating protein
interactions before. So it turns out that if you lower the pH you actually
make the glutenin molecule more charged which means the glutenin
molecules repel each other more which actually lowers the strength of their
interaction which will tend to make the glutenin network more tender. Now
you might say that you don't dump I don't acid. I'm not putting vinegar in
my cake. And there's no acid in baking. But actually that's not true. Acid is
a very, very important part of baking. And to illustrate this I just want to
show you this table which has in it the typical pH's that there are in
ingredients that you might use while baking.

OK,so in our table of common baking ingredients let's start with

vinegar. Of course you don't tend to use vinegar when you bake. But it's a
good acidic ingredient to use as a sort of null. So vinegar has a pH which is
somewhere between 2 and 3 depending on the type of vinegar. So one
common baking ingredient which is quite acidic is buttermilk which has a pH
of 4.5. So another thing that you might add when you're baking often are
fruit ingredients. So for example you might be making an apple pie. And
apples as it turns out have a pH around 3 or 3.1 or so. So depending on
when you put your apples in the recipe if you were to try to actually mix the
apples directly with the gluten when it was developing you would actually
weaken the bonds between the gluten and so on and so forth. This is
something else that you have to keep in mind. And it's a difference between
the different recipes.

So we've talked about the glutenin network. Now let's talk about eggs.
So for this, let's just consider a single egg. You know when you bake, you
put some number of eggs in. And so the question I want to ask is how many
molecules of egg protein are you putting into the batter when you put in one
egg? And I'm going to focus on, just for simplicity, one egg molecule. I'm
going to talk about ovalbumin, which is the major protein component,of egg
whites. You'll remember from earlier in the course, when Dave Arnold talked
about baking, cooking eggs, that there are a huge number of different
proteins that,are involved in gelation networks inside of eggs. And they're all
playing some sort of a role in baking. And I'm just going to focus on the
major one in order to basically inform our thinking about this discussion.
And, in particular, to think about whether or not the egg network can
contribute as much to the elasticity as the glutenin network. I mean, is this
even possible given the numbers of molecules?

So let's think about a single egg. So I'm going to take an egg which
has a volume of about 34 milliliters. That's a volume that an egg can have.
And that actually corresponds to a weight, which is 34 grams, because, of
course, the major component of eggs is water, which has a density of one
gram per cubic centimeter. So an egg white is about 2/3 of an egg. And it
turns out that about 60% percent of the protein in egg white is ovalbumin.
And about 10% of the weight of egg white is protein. So what we have to do
is take the mass of the egg white. We have to divide by 10. That gives us
the mass of protein that's in the egg white. And then we have to multiply
that by 60%. And that basically gives us the mass of ovalbumin. So if I work
that out, 34 grams times 2/3, which is the egg white, times 0.6, times 0.1, I
find that there are about 1.4 grams of ovalbumin in an egg. So ovalbumin
has a molecular weight, which it turns out is about 45,000. And so to
convert that to the number of molecules, where I do is I take 1.36 grams. I
divide by 45,000 grams per mole. I multiply by Avogadro's number, 6.022
times 10 to the 23. And that gives me, let's see. Let me just do this. That
gives me 1.8 times 10 to the 19 molecules. 1.8 times 10 to the 19
molecules. That's a lot of molecules in a single egg.

Now, we need to compare this number with the similar number that
we had,for glutenin. And remember, the way that we did it for glutenin is
we,considered a liter of batter. And so the question that you have to think
about is, well, how many eggs would you put into a liter of batter? Now, if
you're making bread, you would put no eggs in. There tend not to be eggs in
bread. So in eggs, the answer is zero. So if you're making pancakes are
cake, I don't know, it sort of depends on the recipe. But I would say that in a
liter of batter you would use somewhere between, wo and four eggs.
Probably on the higher side, because a liter is actually quite a bit of batter.
So what we have to do is multiply by our number, 1.8 times 10 to the 19, by
four--four because there are four eggs. So that means that 1.8 times 10 to
the 19, that corresponds to about 8 times,10 to the 19 molecules of
ovalbumin in pancakes, and about the same number about 8 times 10 to the
19 in cakes. And if we then convert that to cross-linked distances using the
arithmetic that we did before, that corresponds to a cross-linked distance of
about 20 nanometers or so, a little less than 20 nanometers. The number is
very much in the same ballpark as the distance that we found before
between gluten molecules.

Now, there's one more thing that we have to think about to sort of see
how this thing is going to form a network, which is we have to figure out
how big these ovalbumin molecules are. Now, if you go and look at a crystal
structure of ovalbumin, which is in,its folded state, it turns out the
dimensions of the molecule are about seven nanometers, by five, by five. So
it's actually pretty small. So if you see the ovalbumin molecules were folded
in the batter, if you have something which is about seven nanometers across
and the different things are 20 nanometers apart, they can't stick to each
other. It simply won't work. I mean, if I'm here, and you're on the other side
of the room, and we try to hold hands, we simply can't do it, because our
arms aren't long enough to make the different molecules stick to each other.
However, you will remember from our discussion of eggs before, that the
whole point of actually forming a gelation network in an egg, is that the
protein first unfolds.

And when it unfolds, it will stretch all the way out. If you were going to
estimate how much this seven, by five, by five molecule is going to stretch
out when it unfolds, one way to think about is,just to imagine you stretched
it way out. And maybe the radius of it when it was unfolded was something
like a,nanometer or so. And if you ask how long is something which has a
cross section of about one square nanometer, how long is it going to be? It's
going to be something in the range of about 50 nanometers. So these
ovalbumin molecules, when they unfold, are about 50 nanometers, which is
the same basic length scale that we had for the glutenins. And they will then
be able to stick to each other because they're only less than 20 nanometers
apart. So the conclusion of this is, at least from the egg numbers alone, the
egg network actually seems quite similar to the glutenin network.

If we think about e is equal to u over l cubed, the cross-linked distance

could change a bit. They're not going to be exactly the same in the two
networks. But they're basically the same order of magnitude. The bond
energies are also the same order of magnitude because they're all
interactions, hydrophobic interactions, between proteins modulated by
electric charge. And so one would think that they have roughly the same
consistency at first blush. Now, of course, just to emphasize again, the
structure of baked goods is complicated. There's interplay between the
glutenin networks, the eggs, and also the starch granules, which we now
have to turn. And the way that the elastic modules is actually determined is
by some complex interplay between the three which we can only imagine.

So, finally, let's consider the starch granules. So this part is actually
much easier. So you'll recall from our earlier numbers with the structure of
flour, that we said that 76% of the weight of all-purpose flower is
carbohydrates. That's a rough number. Pancakes are about 40% flour. Bread
is about 60% flour. And cakes are about 30% flour. So that means that the
starch percentage of pancakes is 40%, 0.4, times 0.76. That's about 30%.
So pancakes are about 30% starch. Bread is about 45% starch. And cake is
about 22% starch. So those are the percentages, by volume, off the starch
granules. Now, if you remember our discussion of emulsions from last week,
these percentages are all below the critical percentage that you need for the
granules to actually jam into each other and form an elastic network.

So at first blush, it doesn't look like the starch network is going to

contribute to elasticity. However, when you heat starch granules in a
background of water, they will tend to swell up. You will remember Dave
talked about this, and also Nathan Myhrvold in the,context of reductions of
sauces. The starch granules swell up. The liquid then becomes more viscous
because the starch granules can now bump into each other. Well, if they
continue to swell up, and if the volume fraction of starch granules were big
enough, they will actually form an elastic solid. You will actually have this
network of grains which are actually jamming into each other. And that
network of grains will contribute to the elastic modules. And, indeed, this is
totally within the ballpark of something that can happen in all three of these
recipes. That is in pancakes, in bread, and in cakes, the fraction of starches
within a factor of couple, of two to three of the number, of the volume that it
has to be for it to be able to form an elastic network, swelling by a factor of
two or three is really not out of the question.

So, in summary, what we've just done is argued that the three main
ingredients of cake, bread, pancake recipes, namely glutenin, egg, proteins,
and starch, can actually contribute to the elasticity. We expect from these
numbers for them all to contribute to the,elasticity in some way. And the
precise elastic module presumably depends on the way that you,mix them,
and also the other ingredients that are in the batter, acidic, or salts, or
things like this, which actually can modulate the interactions between them.
I think that the fact that all three of these turned out to be important really
goes some way at least of explaining why this phase diagrams, the bakery
phase diagrams, that I showed you before, are so robust. The fact is that if
you change the amount of flour in a recipe by 10% or,so, you're really not
changing the distance between the glutenin bonds by very much. You're not
changing l at the cross-linked distance by very much. And although that, the
10% change, could affect the recipe-- there are lots of things going on after
all--it's not obviously going to make a huge effect on the elastic networks
that are occurring.

PIA SORENSEN: So throughout this course, we have referred to

browning reactions. When we talked about cooking a steak, we referred to
the browning that, happened on the surface of a steak. And this week, we're
going to talk about the browning that happens in baking.

So in terms of baking, there are really two kinds of browning

reactions, that we're interested in understanding. One is caramelization, and
the other one is Maillard reactions. So let's start with caramelizations.

So caramelization is just what happens when you heat, sugar, white

table sugar. And if you remember back to Carme's crema catalana, you saw
how she sprinkled sugar on top, and then she he heated it to a very high
temperature. And the sugar immediately turned browned, and it created
these very, nutty, caramelly, buttery flavors.

Now here is a demo by Daniel Rosenberg, where he does the same

thing, except he applies way more heat, way more quickly. So he just has a
test tube with white table sugar in it, and as he heats it it turns first brown,
and then it immediately turns black, and it passes, from these nice nutty
flavors that we know from the crema catalana, all the way to sort of bitter,
nutty, vinegary, sticky flavors.

So sugar is just a sucrose molecule. And sucrose is made of fructose

and glucose. And so the first thing that happens when we apply heat is that
these two molecules fall apart into glucose and fructose. And so here is what
these ring structures would look like. And then these ring structures just sort
of explode into a wide array of other small molecules. You can see here the
different molecules. So you can see here is the remainder of the five-ring
structure and of the, six-ring structure. And you can see, then how they've
sort of fallen apart further into, smaller molecules. And all of these
molecules have different flavors, and different smells. And typically, in
caramelization, the flavors that we're talking about are, these sort of sherry,
buttery, nutty flavors. And this happens at temperatures of about 165
degrees Celsius or higher. So if we were to take these flavors and put them
on what we call a flavor, wheel, which is what wine tasters, or tasters in
general, would use when, they would try to guide or pinpointing what the
flavor is-- and, here's a flavor wheel with all of the different flavors,
everything from earthy to nutty to fruity to flowery-- and so caramelization
kind of creates these particular flavors that are sort, of caramelly and nuttybuttery.

And so now keep this in mind, because now we're going to move on to
Maillard reactions and see what kinds of flavors those create.

Maillard reactions, in contrast to caramelization reactions, involve the

reaction between sugars and amino acids. And these typically take place at
temperatures above 120 degrees Celsius. And so what happens here is that
if you, for example, just take milk and heat it, there's going to be sugars in
the milk, and there's going to be, proteins in the milk, amino acids. And the
sugars are going to react with the amino acids and create these browner
compounds that have nutty flavors. And so you've probably had this, if
you've ever had dulce de leche, you've, had this exact same thing. And there
are a lot of desserts and a lot of sauces that sort of build on, this concept of
just heating milk and creating these flavors.

And so there are many different kinds of amino acids. There's about 20
amino acids. And each of them, the first step would be that the glucose
reacts with the amino group on any of the amino acids. So the amino group
is a nucleophile, if you think back to chemistry. And the nucleophile is going
to attack the carbon on the glucose here. And this is then going to form a
bond. And this is kind of the first step in the Maillard reactions. And after
this, there is a whole, again, just an array of different, reactions that can
happen. The molecule falls apart. It reacts again. It reacts with each other,
with other glucoses, with other amino acids. But this is the first step. And so
you can imagine, then, that if there is 20 amino acids, and this is, the first
step, you can just imagine that there is just a lot of different, molecules that
can be created, even with this just being the first step.

The characteristic feature of Maillard products is that they often

contain sulfur and nitrogen, which comes from the amino acids in the
protein. And sulfur in protein often contributes these kind of meaty, earthy
flavors that we associate with when we cook a steak, and there's sort of this
earthy, meaty flavor. And this also then contributes to a lot of the other sort
of non-distinct, flavors that are very different from the flavors that we get in
caramelization.

So here again is the flavor wheel. And I've circled all of the possible
flavors that you can get from Maillard reactions. And as you can see, this
pretty much covers the entire wheel, everything, from the earthy flavors
that we talked about, but also minty, lemony, flowery flavors. And all of this
is possible just from the reaction between glucose and amino acids, which is
pretty amazing.

Another feature that makes Maillard reactions especially interesting

from, a chemical perspective is that they're often exothermic reactions. So
there are two kinds of reactions. There's endothermic and exothermic. And
endothermic are when we need to put in heat for the, reaction to take place.
So when you bake a molten chocolate cake, it's basically an endothermic,
reaction to make it happen. Exothermic reactions produce heat as they
happen. And so as Maillard reactions start to happen, they produce heat,
and this then, leads to more reactions happening. So this speeds up. You
may have experienced this, actually, if you've ever made toast. So
sometimes you may have experienced that you make toast, and you wait
and, wait, and it's not done, and it's not done. And then suddenly it's done,
and then it's done, and then it's overdone. And it just happened very, very
quickly. And this is exactly what happened is that the Maillard reactions
started to take place, and they heat, and then there were so many Maillard
reactions, and this turned to the toast going from a nice, light brown to just
suddenly black. And by the way, as you make toast, there's also the fact that
the temperature increases, and as the toast gets blacker and blacker, there's
also an increase in heat uptake, which speeds up the reactions.

Maillard reactions, of course, are not only in baking. They're basically

everywhere around us. So here are some examples. Everything from coffee
to popcorn to champagne to a nice cured ham are all places where Maillard
reactions have taken place. And in some of these cases, there hasn't even
been an addition of heat. So in champagne, for example, the reaction is
allowed to take place over so long that the reactions take place anyway,
even though there is no input of heat. But all of these sort of earthy flavors
that you get in a champagne or, in meat, they're all also due to Maillard
reactions.

So I think from this we can all conclude that Maillard reactions are,
really yummy, and we preferably just want more of them. So is there a way
that we can just make more Maillard reactions?

So let's look at the chemistry of this to try to figure this out. So we

learned that all of this is due to this amino group attacking the carbon on a
glucose. And so if there's a way that we could just speed up this reaction
and make it happen more, and more often, then presumably, we would also
be able to make more of the later steps in the Maillard reaction. And so if we
look at this, you can think that, let's say you did, something to the amino
group, and you actually made it a better attacker of the carbon, you made it
a better nucleophile, to use chemistry language. And you could do this by
adding a base. And we have talked about a base before in this lecture. And
the base, of course, that should come to mind is baking soda. So baking
soda is sodium bicarbonate. And the bicarbonate, when you add it, it would
take up -- it has a negative, charge, so it would react with the hydrogens.
And you could imagine how it would react with the hydrogens on the amino
group, and this would then make the amino group negative and make it a
better attacker at the carbon on the glucose.

So you could do this with any base. And in fact, when you make
pretzels, you can brush them with sodium hydroxide. And this is what you do
to give them that very dark brown color on the surface, even though the
dough, when you break them open, is actually really light. So you can try
this. And I encourage all of you to go into your kitchen and try this. You can
actually brown onions. And you can try to do this with baking soda and
without baking soda. And you can see if the browning actually does speed up
with the addition of baking soda.

This not only applies to browning onions or to pretzels. It also applies

to baking cookies. So if you look at different cookie recipes, you can
sometimes see that if you were to calculate how much acid and how much
baking soda, ie base, there is and you would sometimes notice that there is
an excess of baking soda in recipes. And basically, any excess of the baking
soda is going to contribute to the browning after it's reacted with the acid to
create gas that increases the leavening.

And so you can then look at different recipes, and I encourage you, to
go and do this. So if you look at recipes for white cookies, you will often see
that there, is baking soda added, but there is also cream of tartar added in
about, the same amounts. And so the idea is that the cream of tartar reacts
with the baking soda, contributing to the leavening, but there's basically no
baking soda left over to contribute to the browning. Whereas in a lot of
cookies where they turn browner upon baking-- and obviously, this depends
on how long you leave something in the oven. If you leave something in the
oven for a long time, it's going to turn brown. But the cookies will get done
without browning if you have the right amount, of acid to balance out the
baking soda. So for example, in the recipe of chocolate chip cookies, there is
baking soda, but there is no cream of tartar to neutralize this. And there's
still acid in the other ingredients, but not enough to, neutralize all of the
baking soda. And this is what's contributing to the browner chocolate chip
cookies.

There are two different ways of producing carbon dioxide gas when
you're baking. The first way, that of using baking soda, Pia described to you
when she explained to you the wonderful rule of thumb that one mole of
baking soda is one mole of carbon dioxide gas. The second way is a bit more
subtle. It involves the addition of yeast to a recipe. This is commonly done
when cooking something like bread, when you take basically a teaspoon of
yeast or so, depending on the recipe, or you use a yeast starter. You put it in
the dough and the yeast, which is, after all a biological organism, produces
gas. So the point of this segment is to explain a little bit about the chemistry
of how this works and to give some context for thinking about how much gas
is produced by the amount of yeast that you put into a baked good.

Yeast are an important ingredient for many aspects of cooking. And in

two weeks, we will have essentially an entire section about the remarkable
things that yeast and other microorganisms can do when we discuss
fermentation reactions. For now what I want to do is observe that the very
same reaction that actually causes grape juice to convert to wine is also
used when baking to create carbon dioxide gas. And that reaction is shown
here. What one does is take a single molecule of glucose and converts it to
two molecules of carbon dioxide and one molecule of ethanol. And this is the
reaction that is typically used. Now yeast, when you put them in the dough,
essentially eat sugar. They eat carbohydrates. And when they digest them,
they convert them to carbon dioxide gas. And that's what causes bread to
rise. So in the same way that we wanted to know how much carbon dioxide
gas was produced from a teaspoon of baking powder or baking soda, we now
want to ask how much carbon dioxide gas is produced from a teaspoon of
baker's yeast.

So one difference between the two is that yeast are living organisms
and produce a continuous stream of carbon dioxide gas. In fact, the rate of
carbon dioxide production that is made by the yeast that you add to your
bread dough is given by the product of the number of yeast that you have
and the rate that each yeast cell actually produce carbon dioxide gas. And so
in order to dissect this, I want to take each of these two factors in turn. So
let's start out with a number of yeast cells that you have. So many recipes
call for a teaspoon or a teaspoon and half of yeast to be added. And so let's
just consider a teaspoon of these and ask how many cells of yeast there are
in the teaspoon. So a teaspoon is about five milliliters, give or take a little,
and what we need to do is take the volume of five milliliters and divide it by
the volume of a yeast cell.

So yeast cells are small things, and it turns out that a typical volume
for a yeast cell is about 50 cubic microns. So that's 50 times a cube, which is
a micron on each side. Now you'll remember that a micron is one ten
thousandth of a centimeter. And so 50 cubic microns is the same is 50 times
10 to the minus 12 cubic centimeters. Now one millimeter is one cubic
centimeter. And so therefore what we need to do is divide five milliliters or
five cubic centimeters by 50 times 10 to the minus 12 cubic centimeters.
And the answer is that we find that there are about 10 to the 11 yeast cells
in that little teaspoon of yeast that you put into your recipe.

OK, so now each yeast cell, each of these 10 to be 11 yeast cells is

basically eating glucose. It's eating the sugar that's in your batter and
producing carbon dioxide gas according to the reaction I just showed you.
And the question of how fast they do this is essentially the question of how
fast does a yeast cell eat. How fast do yeast cells eat? Well, how fast do you
eat? It depends on where you are. If you're in a restaurant full of food you
love, and you're very hungry, you might find yourself eating much faster
than if you're in a place with food that you hate and you're not hungry at all.
The same is true with yeast. Now yeast, of course, don't go to restaurants.
We actually just give yeast carbohydrates and let them be. But how fast
yeast eats depends on how hungry they are and what their environment is
like. And there are, as you would guess, two basic measures of
environmental conditions that influence the rate of yeast growing. One is the
pH and the other is the one temperature.

Now I should say that yeast, just like we have our favorite foods, yeast
have their favorite foods. There are a variety of different sugars and
carbohydrates that yeast are able to metabolize. Glucose is one that they
actually tend to like quite a bit. But the rate that they eat really depends on
what food you give them. Now since we're interested in this fundamental
chemical reaction that involves glucose, so let's focus on the rate that yeast
eat glucose. So we want to have a simple rule of thumb for how fast a yeast
cell might eat. One thing that's very special about yeast is that they divide
every 1 1/2 hours. So that means that essentially every 1 1/2 hours, they
have to double their own weight. Suppose that you wanted to double your
own weight. You may not want to do that. But one thing I think that we will
agree on is that if you wanted to double your own weight, you would have to
eat at least the amount of food which is equal to your weight, because
otherwise where would the mass come from? Now, of course, you have to
eat more than that, but it's a good rule of thumb. If you eat about your
weight of food, then you'll at least have a chance of doubling your weight.

So the way that we're going to estimate how much carbon dioxide gas
the yeast could be creating is to ask how much carbon dioxide gas, if a yeast
cell eats its own weight in sugar. How much do yeast weigh? Well if you
weigh a yeast cell, there's of course two parts. There's the water that's in
the yeast cell, which is not going to come from eating sugar. That's going to
come from drinking. And then there's going to be the other stuff. So it turns
out that the weight of the other stuff-- that's called the dry weight of the
yeast cell-- and that has been measured to be for-- for a typical yeast, it's
about 54 picograms. So that's 54 times 10 to be minus 12 grams. Now
sugar, namely glucose, has a weight which is 18 grams per mole. So 54
picograms is about 3 times 10 to the minus 12 moles of sugar. Multiplying by
Avogadro's number, this corresponds to about 18 times 10 to the 11
molecules. So a single yeast cell is equivalent to about 18 times 10 to the 11
molecules of sugar.

So roughly speaking, we can say then, that if a yeast cell wants to eat
its own weight in sugar, it needs to eat about 18 times 10 to the 11
molecules of sugar. And that will, according to our chemical reaction, convert
to about 36 times 10 to the 11 molecules of carbon dioxide. And this all has
to happen within an hour. So that means that we know that a single yeast
cell can produce, in about an hour, 36 times 10 to the 11 molecules of
carbon dioxide. Now, of course, when you put a teaspoon of yeast into your
recipe, then you put-- we've already argued of order 10 to the 11 yeast
cells. So the total amount of carbon dioxide that can be produced by your
teaspoon of yeast that you somewhat innocuously put into your recipe is 10
to the 11 times 36 times 10 to the 11, which is about 36 times 10 to the 22
molecules of yeast. And that, I mean molecules of carbon dioxide-- and
that's what you could produce in about an hour.

So now the interesting thing, of course, is to compare this number,

which is as I said just an estimate, to the number of molecules of carbon
dioxide that were released when you put in a teaspoon of baking soda. So
Pia had told you that a teaspoon of baking soda is about 0.06 moles of
carbon dioxide gas. And that actually corresponds to 3.6 times 10 to 22
molecules of carbon dioxide. So what we've seen from our simple estimate is
that yeast can produce about a factor of 10 more molecules-- a teaspoon of
yeast can produce about a factor of 10 more molecules of carbon dioxide
then the equivalent amount of baking soda. Of course, yeast also have the
feature that that's what they'll do in an hour, but unless you kill them or do
something bad to them, they will keep producing that gas as time goes on.
So these arguments were just estimates. And I think it would really be very
interesting for someone to do this, do what I talked about, more carefully.
And this would actually be a great topic for a final project of this class. We're
now getting to the part of the semester where you're going to all start
thinking about final projects. And I just wanted to propose one for anyone
out there who is interested.

So what you could do is take a teaspoon of yeast. Put it in a batter

where it actually could eat. Put it in a jar of the sort that Pia showed you in
the baking soda experiment and attach a balloon to the jar, and measure as
a function of time, how much gas is actually produced. It would be
interesting to know how much gas was produced as a function of the
temperature, the pH, that the yeast found themselves in, as a function of
the number of yeast that you put in. And to really start to put together
quantitative rules of thumb for what the rate of production of gas is, from
the yeast that you're putting into your baked good. Of course, as some of
you bakers know, there are various ways of putting in yeast. You can go to
the supermarket and buy yeast, but it's, of course, much better to make a
starter for yourself. And it would be interesting to compare, actually, the gas
production rates of a good starter like, for example, the one that Joanne
Chang showed us that she was using when she made bread with the what
you can get from store-bought yeast.

So another process that is central to baking is that of making bubbles.

You all have the experience of making a cake or making bread or eating a
cake or eating bread and cutting it open and finding that inside there's this
enormous array of bubbles. And you know from your experience that the
bubble and the way that they're structured affects the texture affects the
way that the cake or bread or baked good feels in your mouth. Now, Joanne
showed us when she was showing us how to make cake the importance of
creaming butter for making bubbles. She told us that the way that one
actually gets bubbles or air in general into a batter is by actually mixing the
sugar into the butter. And she described this wonderful thing of the little
sugar crystals being what she called shovels which shoveled out little air
pockets within the butter. That's when the butter gets white and fluffy. And
then when you fold the flour in then you start to have the ingredients of the
batter that you need to make a wonderful cake.

OK, so our goal for today is to think about how these initial seeds of
air or these initial bubbles that are placed into the batter grow and merge
into the remarkable structure of bubbles that you see when the cake is
actually finished. And what we're going to do-- so this is actually a rather
complicated process as you can imagine. There are all of these bubbles
growing. And they're growing for a large number of different factors. But
what we're going to do is focus on a very simple problem. We're going to
imagine that we have a single bubble that is enclosed that is surrounded by
batter. And we're going to talk about the conditions under which the single
bubble grows and what makes them grow how fast they grow and how this
depends on the recipe that you use. And then at the end we're going to
summarize how the lessons that we've learned from this single bubble apply
to thinking about the physics of the entire cake or bread or whatever it is
that you're trying to make.

We've talked about bubbles before in this course. In fact we talked

about them last week in our study of emulsions. And you'll remember that
Dave showed you this wonderful picture of what was then an air bubble that
was surrounded by a liquid. And the air bubble was within the foam. And
what Dave told you about was this concept that he called Laplace pressure.
Laplace pressure was the idea that if you have a bubble energetically the
surface of the bubble costs energy. And it wants to shrink. And so the
surface of the bubble actually tries to pull inwards. It's the effect of so-called
surface tension which then in order for the bubble to remain in equilibrium
has to be balanced by a higher air pressure inside the bubble than outside.
And we wrote down this wonderful equation that says that the pressure
difference across the bubble in order for the bubble to be in equilibrium is
twice the surface tension which we called sigma divided by the radius of the
bubble.

Now when Joanne creamed the sugar there were almost certainly little
tiny air bubbles that were then dispersed throughout the batter after she
was done that came from the little shovels of the sugar crystals that were
making the air. And it's worth thinking for a moment about this Laplace
pressure equation and thinking about what's going to happen. So you see
the surface is curved. And the surface must have a surface tension
associated with it because all surfaces do. And so it wants to close. And so
an interesting question to think to yourself is why does it not close? That is
why do the bubbles not close up upon themselves? And there are from what
I can tell only two possible answers to that. And I should say I don't know if
this is right.

But I can only see two possible answers. So one is is that as Dave also
told you last week one can sort of get rid of the surface tension of an
interface by adding surfactants. So surfactants are of course proteins which
have one side that like to live on one part of the interface and the other side
that likes to live on the other part of the interface. And if you pack the
surfactants around the outside of a bubble you can stop it from closing. So
you can ask yourself does the batter that Joanne used have any surfactants
in it? And the answer is of course yes because she used butter. And butter is
a milk product. And milk has proteins within them which absolutely are
surfactants. There are the casein proteins for example which might be
coating the bubbles in the batter after she makes it. So that's one possible
explanation that he surfactants are protecting the bubbles from closing. The
other possible explanation is that actually the bubbles are just closing that
the batter is so viscous it's so hard to make flow that the forces that are
causing it to flow are small enough that it just takes a long time for them to
close and long enough in particular for you to go forth and cook your cake or
bread or whatever it is that you're going after.

OK, so let's recall what Pia told us. She told us that one teaspoon of
baking soda corresponds to about 0.06 moles of carbon dioxide gas. And if
you multiply it out you will discover that corresponds to about 2.6 grams of
carbon dioxide. So in the batter that Joanne made there were about 2.6
grams of carbon dioxide gas. And the question that we have to ask is where
does it go?

So from what I can tell there are basically three possibilities. First of all
the gas could dissolve in the liquid. The batter is after all composed of liquid.
And in principle the carbon dioxide could dissolve there. Secondly the gas
could go into bubbles. It could cause the bubbles to puff up. It must get in
the bubbles eventually because we know that's what happened in the cake.
But that doesn't mean that it goes in initially. We have to think about that.
The third possibility is that of course the gas could escape. It could get out
of the cake entirely and not be useful for baking.

So let's think about the third one, number three, first. Thats in a
way the most difficult but it's also the simplest to dismiss. So it's certainly
the case that in cakes some of the gas is going to escape. We don't really
know how much of the gas is going to escape. But some of it simply has to
escape during the baking of a cake. You can sort of estimate that based on
what Pia told you. I mean if you had two liters of batter and you produce a
liter of gas you can measure the volume of your cake afterwards and see if
it's smaller than three liters. I'm sure that it is. And that's sort of the
amount of gas that you must have lost. On the other hand its worth
noting at this point that in baked goods not as much gas is lost.

So, for example, youll recall Joanne's demonstration for us of

bread making. And there she showed us the little bubbles that form on the
outside of bread. The gluten is so strong that the bubbles actually just
expand under the pressure of the gas. The gas there of course comes from
yeast. It doesn't come from carbon dioxide. But anyway its still gas. And
those bubbles are -- and there, gas is actually being trapped more clearly in
order to keep the bread dough rising.

So let's now turn to reason number one, which is dissolution. So how

much of the carbon dioxide gas the one-liter of carbon dioxide gas that's
produced in this recipe actually dissolves in the batter? So in order to see
this what we need to do is revisit an old friend, a concept that we discussed
in week three of this course. Hopefully, you all remember back that far.
There we talked about solubility. And we talked about the fact that molecules
could dissolve in a liquid. And the amount that they could dissolve was called
the solubility. We made an analogy to that of an actual gas youd recall
in week three.

So let me show you here in this plot the solubility of carbon dioxide
gas in water as a function of temperature because you know of course that
when you're baking youre starting out at about 23 degrees or so. And
clearly the cake heats up to well above 60 degrees if not hotter in the center
as it cooks depending on exactly your recipe and heating protocol. Now, at
room temperature it turns out that about 1.5 grams of carbon dioxide
dissolves in a liter a batter 1.5 grams. And whereas if you go up to a much
higher temperature-- so another reasonable temperature to look at is 60
degrees because that's the temperature where egg start denaturing and
these reactions start occurring-- and there its about 1/2 a gram of
carbon dioxide.

So what does this mean for Joanne's recipe? Well remember

Joannes recipe had two liters of batter in it. And so in two liters of batter
at room temperature that means you can dissolve about 3 grams of carbon
dioxide gas. Well thats more gas than actually is produced by the baking
soda reaction. So this is sort of remarkable. So it means that initially the
baking soda is essentially going to be-- the carbon dioxide gas from the
baking soda is going to be dissolved in the batter. I mean we don't know this
for sure I should say. We've never gone and looked. But if you think about
it the reactions must be I guess occurring within the batter. And it's
certainly reasonable-- which are in the liquid that is to say-- and so it's
reasonable to imagine that the gas is initially just completely dissolved in the
liquid. So this means that initially in the batter the gases in the liquid you're
not actually pressurizing the air bubbles the little bubbles that you've made
at all. They're just sort of hanging out for the ride.

Now as you start to heat the cake though the situation changes
because then the solubility goes down. And when the solubility goes down
the molecules of gas in the batter have to go out. And they start to fill up
the bubble. And when they fill up the bubble now the pressure in the bubble
is larger than it was before. And this of course will cause the bubble to
expand. So what you must admit about this process that I've just described
is that it's really very subtle. Initially the dissolved CO2 is stuck in solution.
And depending on how you heat it will start to out gas and expand the
bubbles. Now while the bubbles are expanding they are out of equilibrium.
And so it's now not true that the pressure difference between the inside and
outside of the bubble is balanced with the surface tension. If that were true
the bubble wouldn't grow. Instead these two are unbalanced. The pressure
difference delta P -- P out minus P in -- is bigger than 2 sigma over R. And
so something must balance that mismatch. And indeed the thing that
balances it is our good friend from two weeks ago--the viscous stress--because you see as the bubble grows its actually pushing the batter
around it out. And that's producing a viscous stress, which is sort of the drag
force that's slowing down the growth of the bubble.

And so we can write this down as an equation. We can write down

viscous stress-- that is from the drag of the growing bubble-- is equal to the
pressure difference-- P out minus P in-- minus the surface tension force
which is 2 sigma over R. And these words can be translated into symbols. It
so happens that the viscous stress if we say that the bubble has radius R
and the velocity of the bubble-- the bubble is expanding at a velocity V-- we
can write the viscous stress as 4 times the viscosity eta that we talked about
last week times V over R. V over R you might recognize as being the sheer
rate that we talked about when we talked about viscosity. And so this
formula for eta times V over R is really the viscosity times the sheer rate,
which youll remember from before from two weeks ago, is the viscous
stress. So we can take this equation and we can solve for V the velocity of
the bubble. The velocity of the bubble is delta P that is the pressure inside
the bubble minus the pressure outside times the radius minus 2 sigma the
whole thing over 4 times the viscosity eta.

And so, this formula, what it contains within it is everything that you
need to know about how the bubble grows. And we can use it to think about
the various scenarios that might occur when you bake. So let's start out with
the situation at hand. Namely were under the assumption that all of the
carbon dioxide gas is initially dissolved in the batter. When you heat up the
batter then there will be outgassing of the carbon dioxide gas. This occurs as
I said before because of the solubility curve of carbon dioxide gas. And by
the time you get up to 60 degrees Celsius we know that the solubility will be
cut by about a factor of 3. And so there will be a lot of gas released. And
this will cause the bubble to grow. Now the gas that's released though
wont all be released at once because of course its only coming out
as we heat it. So it's going to be gradually released. As you increase the
temperature by a little bit therell be a little more gas released and a
little bit more. There'll be a little more gas released and so on and so forth.

And so what this equation will tell us is that you know that delta P will
increase a little and the bubble will grow and Increase a little more and the
bubble will grow. And that will continue until the end of the recipe. That
appears to be the situation in the recipe that Joanne gave us. So there's
more feature that I want to mention of this equation and just really
emphasize the complexity of baking. So remember everything is going to
change as we heat the cake. It's not just the outgassing of carbon dioxide.
It's also the material constants themselves. Eta, the viscosity, is going to
change as we heat the batter. Generally, when you heat things viscosities
decrease, which means it, becomes easier to expand as they get heated.
However in a cake as we've already discussed the situation is complicated
because in addition to making the batter itself less viscous one is also
producing elastic cross-links between the gluten in molecules and the egg
proteins. And this is actually making the batter more elastic. And we haven't
talked about that at all.

Now if we think about elasticity if I have this bubble and the bubble
were growing into an elastic medium the elasticity of course will act to
squish back on it. It will not want the bubble to grow. And it will constrain
bubble growth. And so depending on the temperature curve-- that is how
you're heating the cake-- the batter will at some point become elastic and
also stop about the bubble growths. Hopefully the summary of this for all of
you is that the situation from the point of view of physics is really very
complicated. And it's no wonder it takes such talent to cook a good cake. I
mean so the cake bakes and as the cake bakes as the batter heats up we
change the solubility of carbon dioxide, which changes the amount of gas
that's around.

Remember, I haven't even talked about the release of water vapor.

That also occurs as you're heating and is well known to be an important part
of baking. Water vapor evaporation of course occurs with a different rate
than the gas solubility constants because the phase behavior of water is just
different. The viscosity decreases of the batter with the function of
temperature. I assert that because that's what generally happens to the
viscosity of things when you heat them whereas in the case of a cake the
elasticity will increase because all of this elastic network that we've talked
about will start to grow. Getting this right in your cake recipe or your bread
recipe is absolutely critical in order to end up with the texture that you need.
And at least for me this situation starts to explain why it is so hard to bake a
cake. And I should say just as a final note that I focused on the case of only
one bubble. But in reality there are lots of bubbles that are growing all over
the place that is each going through a process like what I've just said. And
they of course are going to interact with each other in some complicated way
which sort of goes beyond this simple discussion that I've just given. Some
of you might not think it's simple but could have been worse.

How hard is it really to make a great cookie? After all it's one of the
first recipes that many of us make as kids. Yet while cookies may look simple
they're actually surprisingly complex. Even very small changes in ingredient
quantities or mixing method can yield significant differences in flavor and
texture. You'll see exactly what I mean as I show you how the test kitchen
re-engineered the All-American chocolate chip cookie. We wanted better
flavor and better texture. Now what do I mean by better flavor? We wanted
far more complexity more toffee and butterscotch notes which really
balances the sweetness. As for texture we wanted really crisp edges that
would contrast with the moist chewy center.

And here's how we did it. Most chocolate chip cookie recipes start by
creaming softened butter with sugar. Now the goal of creaming is to beat
tiny pockets of air into the butter, which will then fill with gas and steam
during baking. The result of this mixing method is a cookie with a higher rise
and a cakier interior. But what if you're after a chewy cookie and not a cakey
one? Well then you don't want to cream the butter but rather melt it. Not
only is melting the butter easier you don't need to break out a stand mixer it
also produces chewier cookies. One reason is that butter contains about
18% water which when freed from the butter during melting mixes with the
flower and the dough and forms gluten which provides chew. In addition
melted butter means less air pockets because we're not creaming so less
unwanted rise we get denser chewier cookies. The effect of melted butter
can be seen in many classic cookies including molasses spice oatmeal raisin
and peanut butter cookies.

So starting with melted butter is a really good first step. But for our
recipe we took things a little bit further by browning the butter as well.
Brown butter what the French call burre noisette or hazelnut butter displays
the complex aroma and flavor of nuts. It's an amazing transformation that
we owe to the Maillard reaction, which is the same process that give us that
crust on a nice seared steak. Butter is an emulsion of water in fat which
breaks upon melting in the pan. Milk proteins and sugars that are in the
butter then fry in the butter fat. And this is what produces hundreds of new
flavor compounds. The good news is it's also very easy to do. So you want to
make sure to use a light-colored skill like this point here. Using a non-stick
skillet it's simply too dark. We won't notice the color change. So I'm going to
add my butter. You want to use medium heat which is going to be a little bit
more gentle. The other key is you want to make sure your swirling the pan
so that the milk solids brown evenly. So first I'm going to let this melt. And
then we will watch that transformation take place. OK, you can see that the
butter is melted. Now some of that water that's come out of water is now
evaporating. At this point you want to start swirling. Thats going to
allow that water to evaporate without making the hot fat pop out at the pan
at you. You can also see some of the white milk solid starting to separate.
Theyre on the surface right now. But they will eventually settle to the
bottom where theyre going to start to brown. OK, you can see that it's
definitely starting to darken. And it really smells. I can smell kind of a nutty
hazelnut aroma. All right that's looking pretty good.

Now, the trick with brown butter is that as soon as its at the color you
want you need to get it out of the pan. Im going to transfer it to this
heat proof bowl here. There's a lot of residual heat in this. So it's going to
continue to brown even now that I've dropped it in here. So what I'm going
to do is I have 10 tablespoons of butter in here. I'm actually going to add
four more that haven't been browned. Im going to stir these which is
going to cool down the whole mixture which is great. The color won't
continue to darken. Its also adding back some water which we really
drove off a lot of while we were browning the butter. So I'll stir this until it's
totally cool. All right great it is all melted into it and our butter is cooled
down. OK, so I set that butter aside.

Now let's talk a little bit about the sugar in our recipe. We often think
of sugar as providing sweetness which it certainly does. But it also drastically
affects the texture of baked goods. Thats because sugar has an affinity
for water. Its hygroscopic. The hydrogen and oxygen molecules in sugar
and water are electrostatically attracted to each other so they link together
to form hydrogen bonds which are very hard to break. As a result sugar
slows the evaporation of moisture from cookie dough or cake batter ensuring
a final product that is moist and tender. Now all sweeteners are not created
equal. If you use brown sugar rather than white sugar in a cookie you not
only end up with a different flavor but also a different texture. Why?
Granulated sugar is pure sucrose. Brown sugar is sucrose with some invert
sugar. Sweeteners with a lot of invert sugar now think honey molasses and
even the molasses in brown sugar are liquid. They have a very hard time
crystallizing like sucrose. And invert sugar is even more hygroscopic or
water-loving than sucrose. It can even draw in moisture from the air after a
cookie is baked to keep it moist.

So to demonstrate the effect of invert sugar in brown sugar I've made

two oatmeal cookies one with white sugar and one with brown sugar. Look
what happens when I try to get the cooled cookies to conform to the
curvature of a rolling pin. This is the white sugar cookie. Now the brown
sugar cookie contains a lot more moisture and bends right around the pin.
And that makes for a very chewy cookie. The classic toll house chocolate
chip cookie recipe calls for equal amounts white and brown sugar. To get the
full benefit of invert sugar we switched to three parts brown sugar to two
parts granulated sugar. So that's 3/4 a cup of dark brown sugar and a half a
cup of granulated sugar. Now, we tried using all brown sugar but it's flavor
was really overpowering.

But perhaps even more important than the ratio of the two sugars is
how we added them to the butter. It turns out that sugar that is dissolved in
liquid before baking caramelizes more readily than sugar that simply
dissolves in the oven. For our perfect chocolate chip cookies we let the wet
ingredients in the batter rest for 10 minutes whisking occasionally in order to
dissolve the sugar. This step helps break down large sucrose molecules into
smaller glucose and fructose molecules which caramelize at lower oven
temperatures. So, we're in effect creating more invert sugar out of the
granulated sugar. And as we now know more invert sugar equals more
caramelization and thus more flavor. So, I'm going to add my brown sugar
which is 3/4 of a cup of dark brown half a cup of granulated sugar. Im
also adding a teaspoon of table salt and a full two teaspoons of vanilla
extract. So I'll whisk these into my brown butter until smooth. And at this
point you really want to break up any big chunks of brown sugar.

OK, so now I'm going to add my eggs. And I'm actually using one
whole egg and one yoke. The classic recipe on the back of the Nestle bag
calls for two whole eggs. But that extra egg white protein can lead to a
cookie that is cakey instead of nice and chewy and dense. Im going to
break these up and whisk it in. Now, this egg is bringing with it a lot of
water. And that's going to allow the sugar to dissolve. OK, so I've whisked
this for about 30 seconds. And as you can see it's a lot smoother. Now I'm
going to let it rest for about three minutes whisk again for 30 seconds and
repeat that a couple more times. What we're doing during this 10 minute
resting period is allowing a lot of that sucrose to break into glucose and
fructose. More of it's going to dissolve. And we're going to get cookies with
better browning. So, with this method, as these cookies bake the oven is
going to evaporate moisture from the perimeter of the cookie first while the
remaining moisture is going to be retained in the center. Now that disparity
is what will give us great contrast in texture from a crisp rim to a chewy
center.

While I wait for the sugars to dissolve I'm going to get the flower and
leavener ready. In addition to the fat and how it's treated and the sugar and
how it's treated the leavening agent makes a huge difference in the texture
of cookies. Now, we basically have two choices: baking soda and baking
powder. Baking soda reacts with acidic ingredients such as sour cream brown
sugar or molasses in a batter or dough to create carbon dioxide. As soon as
the baking soda comes in contact with liquid it reacts. So, as a result, it
doesn't have much of an impact on rise during baking. Baking powder on the
other hand is baking soda mixed with a dry acid such as cream of tartar and
double dried corn starch. The cornstarch absorbs moisture and keeps the
baking soda and the dry acid from reacting until they become wet. Most
baking powder that you find today is double acting. So there are two dry
acids. And one which is usually sodium aluminum sulfate is heat-activated
above 120 degrees. This means that we get an extra boost of leavening once
the cookies go into the oven. This additional rise is great for lots of baked
goods.

Many cookies are made with leavener. Some are made with both. The
decision should be made based on the dough's other ingredients. For
example is there an acid available to react with the baking soda? As well as
what the desired final texture of the cookie is. So for our chocolate chip
cookies we just have baking soda. Why? In addition the less rise baking soda
also helps with browning which is something we want. Caramelization and
browning occur best in an alkaline environment. So amino acid molecules
like those found in flour have two ends the amino end and the acid end. The
acid end is acidic. The amino end is alkaline. So it's the alkaline end that has
to react with the sugar molecules for the Maillard reaction to occur. In an
acidic dough, the alkaline ends are basically deactivated. However, in an
alkaline dough created by the addition of baking soda, the amino ends
thrive. And they can react with the sugar to create browning.

So I'm going to add my flour. And this is 1 and 3/4 cups of all-purpose
flower and half a teaspoon of baking soda. And I'm just going to whip these
together. Theres no need to set sift ingredients. OK so now I'm going to
add my flower to my butter and sugar mixture just after about 10 minutes.
And here I'm just going to stir the two together. Im using a wide spatula
so you can get underneath the batter pull up any of the dry flour that's
sitting down there. OK so that's just combined. Now we're going to add our
chocolate. These are chocolate chip cookies so it's pretty important.
Were using 1 and 1/4 cups of chocolate chunks. So it's basically a
bittersweet chocolate bar that we've chopped up. We really like these nice
big pieces of chocolate. Now I'm just going to fold this together so we get
good even distribution of the chocolate.

All right that looks good. So we've got our dough together. But we're
not quite done. For chewy cookies you need to portion the dough carefully.
In general, the larger the cookie the better the contrast between the chewy
center and the crisp exterior. For this reason we use about three tablespoons
of dough for each cookie. Im actually going to do this using a portion
scoop. Now there are many different sizes of them. They look like small ice
cream scoops. They all have a number that determines how big they are. So
for this recipe you want a 24 portion scoop which is about three tablespoons.
So I'm going to portion these out. And right now I'm just transferring them
to a lightly-greased baking sheet. OK so now I'm going to roll these into
balls. And I'm going to transfer them to two baking sheets two rimmed
baking sheets that I've lined with parchment paper. And what I want to do is
space them about two inches apart which will give them plenty of room to
spread.

OK so my cookies are portioned out. And it's almost time to bake. Now
up to this point we've worked really hard to create a dough that will yield
chewy cookies. And it's important that we don't throw it all away by baking
these cookies for too long. I'm going to put them in a 375 degree oven on
the middle rack one tray at a time for about 10 to 12 minutes. And once the
edges are golden brown and set the cookies are done. The center will still
look soft. And it's going to look under-baked. But that's OK. That's the point.
Were going to let the cookies cool on the baking sheet where residual
heat in the pan will ensure that the center sets up just enough but still
remains chewy. So I'm actually setting my timer for five minutes which is
the halfway mark. Now at that point I'm going to rotate the baking sheet to
ensure that they brown evenly all over.

OK so while our cookies bake let's talk a little bit about baking sheets.
And believe it or not the type of baking sheet really matters a lot when
youre making cookies. The material will really affect baking time a lot
with darker sheets browning cookies much faster than light ones. Even the
presence or absence of rims on a baking sheet will change baking time.
Sheets with no rims allow for greater air circulation and faster cooking than
rimmed baking sheet. To prove the point I've baked two identical batches of
sugar cookies. Now these two sheets in front of me were both baked for the
same length of time in the same oven one after another at the same oven
temperature and on the same rack. The one inch rims all around this baking
sheet diverted some of the hot air in the oven. Now as you can see these
cookies are a lot lighter than these cookies over here which baked without
rims. You can get similar results. You just really need to adjust baking time.
So these cookies baked for about 10 minutes. As you can see we have some
good browning around the outside. The center still looks very raw. Thats
good. Were going to let them sit. Cool on the tray. And we're going to
have cookies with a nice crispy exterior and a good chewy inside. Now I
actually have a few cookies that I baked before. So we can see nice and
chewy with a really nice crisp exterior. So the great thing about these
cookies beyond their nice texture is that you have a lot more that
butterscotch flavor from the way that we treated the sugar. We got a lot
more Maillard reaction in the oven. So they're a lot more balanced.
Theyre not just sweet. This is a real classic.

Surface Energy

28/11/2013 13:09:00

This week we're going to talk about emulsions and foams, which are
perhaps

much more common in food and cooking than you may think.

We're going to visit Nandu Jubany in his restaurant in Spain, and

Nandu

will show us some of his dishes that involve emulsions and foams.

One of my favorites is his garlic aioli dish, which he's able to make

with oil and garlic alone, a beautiful aioli.

For us, though, he will put in a little bit of egg, which, for reasons

that we will explain, will make the recipe easier to

make and less pungent.

He will also make Hollandaise sauce, and he will tell us his secret tricks

for how he prevents the sauce from breaking.

And then he's going to tell us how to make carrot foam and a delicious

oyster foam.

And we will use these creations as motivation to delve deeply into the

physics of emulsions and foams, how they work, how they fail, and
how

you
can prevent that in the kitchen.
We will also return to Carles Tejedor's olive oil gummies, which, as
it turns out, are emulsions, and now we can understand them more
deeply.

We will visit America's Test Kitchen, who will show us their recipe for

angel food cake.

The first step of making their angel food cake involves making a
wonderful,

puffy egg white foam.

And they will show you how to make a foam without weeping or
dripping.

And of course, Harold McGee will visit us, and he will tell us about his

special insights on emulsions and foams.

At the end of this week, you will know that an emulsion is a mixture of
droplets of one fluid immersed in another.
And a foam is a mixture of air bubbles within a liquid.
The difficulty of making a foam is that the interfaces cost energy.
There are lots of interfaces on the surface of the droplets or air
bubbles

that you have in your emulsion or foam.

And as a way to stabilizing these interfaces, we use surfactants.

And this week, we'll learn more about what they are and how they
work.

Finally, we will learn that foams and emulsions can become solids
when the

volume fraction of the air bubbles or of the droplets get to be high

enough.

The different droplets and bubbles can support each other and make
what was previously a liquid into a stiff solid.

And finally this week, you are going to be experimenting with

emulsions and

foams yourself by making mayonnaise in your kitchen and by

experimenting with egg white foams.

Let's get going.

DAVID WEITZ: So here's an example of emulsions and foams, which is

what, we're going to talk about this week. What do these things have in
common? Look, there are four examples here. There's a mayonnaise, there's
an aioli. That's two examples. In this case, they're drops of one fluid,
probably oil, in a second fluid, probably water. Drops of oil and water. The
other two examples are foams. There's cappuccino, it has foamed milk on
top or whipped cream, which also is foam. In this case, they're drops of air
or a gas inside a continuous fluid.

So an emulsion is drops of an immiscible fluid in a second fluid. Drops

of one fluid in a second fluid. A foam is the same thing, except, instead of
using a fluid on the inside, of the drops, you use air, a gas.

So how do you make an emulsion? What really is an emulsion? Well,

the best way I can show is to do a little experiment. Here I have olive oil and
water. And I'm going to try to mix them together. And olive oil is not mixable
in water. And when I pour the olive oil onto the water, it floats on top, it's
lighter, than the water. So the only way I can mix them is to shake them. So
let me shake them like this. And look, they do mix, but they don't
completely mix. Instead, you form drops of the oil in the water. And that's an
emulsion. But let's watch this for a little while. We put it on the side.
Remember, the oil is lighter than the water and it's going to start to float, to
the top. And as it floats, the drops become closer and closer. And they begin
to join together and they lose their stability. The emulsion doesn't remain
drops of one fluid or another, but rather phase separates, becomes the two
fluids again. And if you look at them, if we watch them over time, you'd see,
they'd, completely phase separate. In this case, if we wait just a little while,
you see that one fluid collects, on the bottom, this is the water, and the
drops are collecting and forming in oil on the top. They begin to phase
separate.

So this emulsion is not stable. So how do we make an emulsion? An

emulsion is mixture of one fluid in a second by making drops. For example,
in this case, we've made oil drops in water. The oil drops are now called the
dispersed phase. There the drops dispersed in the continuous phase of the
water. The water is called the continuous phase. And to make an emulsion,
you have to mix them together. Somehow you have to form drops of the
dispersed phase in the continuous phase. When you do that, you get these
drops, and that's your emulsion. But to make them stable, you have to
prevent the drops, you have to keep, the drops as individual drops. You can't
allow them to join together, or coalesce.

So small drops become larger drops, and larger drops become still
larger drops. And eventually, they completely phase separate and go back to
the original two phase separated fluids. Somehow, you have to stabilize the
interface of the drops of the oil in the water. And we do that using a
surfactant.

A surfactant is a surface active molecule. It's an amphiphilic molecule.

It has both water-like and oil-like properties. Part of it is water-like, or
hydrophilic, and the other part is oil-like, or hydrophobic. And they're joined
together, they're chemically bound together. So the surfactant molecules like
both the oil and the water. And they can't really decide which they want. So
they can't really sit in either the oil or the water. Instead, they prefer to sit
at the interface, at the surface between the two fluids.

And if you have enough surfactant, an egg yolk, for example, is an

excellent surfactant, they completely coat all of the interfaces. And then,
when drops come together, as I show here in this little cartoon, when two
drops come together with a coated interface, with a surfactant-covered
interface, the surfactant acts as a cover, a covering, of the surface. It
prevents the drops from joining together and becoming larger drops. So the
drops remain st

AVID WEITZ: We saw Nandu make one of the most delicious, most
impressive, kinds of emulsions, aioli. Aioli is like a garlic mayonnaise. It has
very simple ingredients, it's garlic, salt, and olive oil.

And what he does is he mixes the salt with the garlic, and he crushes
the garlic. The salt pulls the water out of the garlic. And then the water from
the garlic acts to emulsify the olive oil. The garlic itself, the remnants of the
garlic, that crushed garlic, act as a surfactant to stabilize the drops of the
olive oil in the water. And you saw Nandu slowly mix them together, he
crushed the garlic, he pulled the water out, and he slowly mixed the olive oil
in, slowly, emulsified it.

And ultimately, he made a solid emulsion. The only way they emulsion
can be solid is if he emulsifies sufficient olive oil that you get these highlycompressed drops so they become elastic, they become solid.

But the amazing thing is the garlic is the only thing that's serving as a
surfactant, and the water from the garlic is serving as the continuous phase.
And if you watch Nandu make it, sometimes what he'll do is he'll say that the
emulsion is about to break, just as he's finishing it. He'll listen to it and say,
it might break. And then he takes a few drops of water and adds it to the
emulsion.

The reason for that is that you're so close to phase inversion, you have
so much olive oil in so little water, that it can easily phase invert. And
instead of having drops of oil in the water, you have huge numbers of drops
of oil in a relatively small amount of water, instead it can phase invert, and
you can end up with drops of water in oil. Then you have a very small
amount of water as drops in oil, but you don't have an emulsion and you
don't have a solid.

So when he hears the emulsion's about to break, he adds a little extra

water. Now, a simpler way of making an aioli is to add a surfactant. Garlic is
not the best surfactant, that's why it's very difficult to make a true aioli. To
make it much more easily, what Nandu did was he added a really wonderful
surfactant, and that's the yolk of an egg. So he took an egg yolk, he mixed it
with the garlic and the water, and that then could much more easily emulsify
all of the olive oil.

Without the egg yolk it's called aioli, and that's the most simple form
of an emulsion. It's also to me one of the most impressive forms of an
emulsion, because it's so little, so few ingredients, and yet you get this solid
garlic-like mayonnaise.able, and the emotional remains stable.

DAVID WEITZ: An essential feature of emulsions is the fact that you

have lots and lots of interface between two fluids. So for example, if you
disperse oil and water, you have to make lots of interface for the bubbles of
the oil to be dispersed on the water. And whenever you create new interface,
you have to put energy in. Whenever there's an interface between two
fluids, there's an energy, there's a surface energy. This is what leads to
surface tension. There's a force that tries to pull the fluids together. That's
called the surface tension. That's the result of the fact that you've created
this new interface and you have to put energy in.

So the surface tension is the same as the surface energy. The surface
tension is force per length, that's a tension. The surface energy is exactly
the same, if I multiply force by a length, I get energy. And if I multiply
length by length I get an area. So the surface tension is exactly the same as
a surface energy - it's energy per unit area. So for example, the surface
tension between oil and water is typically 70 millinewtons per meter. That's a
force per length. You can also think of it as an energy, it's 70 millijoules per
meter squared, an energy density, an energy per unit area. That's what a
surface tension is - it's the amount of energy it takes to create the new
interface. And we can think of this as a natural thing. What is the interaction
energy between the molecules? And what is the area? That's the
macroscopic view of what a surface tension or a surface energy is.

So for example, I draw here an interface between oil and water where
I show the individual molecules of the oil and the individual molecules of the
water. And the surface tension, the surface energy is just the energy per
molecule. So there's a certain interaction energy between the molecules that
gives me this energy term, the U. And there's an area, it's just the diameter
square of each of the molecules. And that gives me the area of the molecule.
So the surface tension is just the energy per unit molecule.

I can actually calculate that for a water-oil interface. Let me just

calculate the surface tension due to the water. I can do that by saying, what
is the interaction energy between the water molecules? Well, I know the
water molecules can move very freely, they can move around, so they can't
have a very large interaction energy between them. So I'll just use the
simplest thing I can, I'll just use thermal energy as the energy of interaction.
And then I will calculate what the area is. I'll take as a typical water
molecule, I'll take a dimension, say, of two ngstroms. And if I do this and I
calculate the surface energy, which is just the thermal energy divided by the
square of two angstroms, I come up with the value of 100 millinewtons per
meter or 100 millijoules per meter squared. That's very, very close to the
value that you actually measure for an oil-water interface, which is 70
millijoules per meter squared.

And the surfactant, we need a surfactant to stabilize these interface.

The surfactant is an amphiphilic molecule, it goes to the interface. But the
main role of the surfactant in terms of the surface energy is that it has
typically a larger dimension than the water or the oil. So the energy now is
still the same interaction energy, it's still the, thermal energy, but the area is
larger. And so, for example, we can calculate the surface tension of a typical
surfactant molecule. A surfactant molecule might have a dimension, say, of
about three ngstroms. And if we calculate what the change in the surface
energy is, it's just now thermal energy divided by three ngstroms. And we
get something about 50 millinewtons per meter or 50 milijoules per meter
squared. It lowers the surface tension. And that's very much what a
surfactant does. It always lowers the surface tension or lowers the surface
energy. And it does that just because it's a larger molecule.

However, the main role of the surfactant in creating and emulsion is,
not to lead to a lower surface energy. Instead, it's to create a more stable
interface. So the surfactant coats the interface and prevents coalescence,
prevents the drops from colliding with each other and joining together and
forming a larger drop.

So for example, when Nandu used egg to make the aioli, egg is a
wonderful surfactant, it's one of the best surfactants there are. And that is
not to reduce the surface tension - it certainly does reduce the surface
tension - but the main point of using the egg is to stabilize the interface
between the oil and the water and to make the aioli stable, much more
simply than it would be in the absence of egg.

DAVID WEITZ: The surfactants, or amphiphilic molecules they want to

sit at the interface. Typically, you put the surfactant in the continuous phase.
So if you have an oil and water emulsion you put the, surfactant in the
water. The surfactant likes to sit at the oil and water interface. So part of the
surfactant sits at the oil. There's excess surfactant, however, you need to
have excess surfactant, so that you always have more surfactant available,
so that it can come to the interface as you create the interface when you're
emulsifying something.

The surfactant has to come out of the water and go to the interface.
However, the surfactant does not like to stay in the water, because it has a
part of it which is oil-like. It doesn't like to be in water. So instead, the
surfactant forms aggregates, we call these micelles. They aggregate so that
the tail groups, the oil part of the surfactants are all connected together,
they're all facing one another, excluding some of the water.

So the surfactant itself forms these aggregates that are called

micelles, that allow the surfactant to exist in the water without exposing the
tail groups to the water itself. But the micelles act as a reservoir. They can
easily break up and bring new surfactant to the interface as you create the
interface.

So whenever you have a surface tension or surface energy, you always

want to find the shape that minimizes the energy. You minimize the energy
by having the shape that has the least surface area. And that shape is a
sphere. A sphere has the least area for its volume, as compared to any other
shape. That's the reason why, if you have an emulsion, the emulsion drops
are always spherical. You're minimizing energy, because you have this
excess energy at the interface.

Another thing that happens is the drop wants to pull in on itself. That
force has to be resisted by something, so, in fact, there's a pressure on the
inside that has to be a little bit larger than the pressure on the outside. This
pressure difference is called the Laplace pressure. And we can calculate that
in a very simple way. We can just balance the forces due to the surface
tension with the force due to this difference in pressure.

So if we calculate the force due to the surface tension, it's the surface
tension times the circumference of the drop, 2*pi times the radius of the
drop. And that has to be balanced by the force due to this pressure
difference. That is I take the pressure on the inside minus the pressure on
the outside, I multiply that by the area of the drop. So it's pi times R
squared. I set these forces equal, and what I do I can calculate then what
the Laplace pressure is.

The Laplace pressure is just the difference in pressure of the inside,

how much greater it has to be from the outside. It has to be larger, because
the surface tension is pulling everything in. So I calculate that and find that
it's 2 times the surface tension divided by the radius of that drop. That's the
Laplace pressure. That's the excess pressure on the inside that's trying to
keep the drop blown up.

You can think of it in a very simple way. If you have a balloon, a

balloon has an elasticity to, it's slightly different from the surface tension,
but it plays exactly the same role. And in order to get the balloon blown up,
I have to put excess pressure in, I have to blow it up. And that pressure is
exactly the same as the Laplace pressure inside the drop, inside the
emulsion drop. So I can calculate what the effect is, and because I have this
excess pressure, because I'm blowing the drop up, if I take two drops and
now squeeze them together, and push them together -- think of taking two
balloons and pushing them together -- in order to deform the shape, I have
to put a force on. I have to deform it. I have to squeeze them together.

The same thing happens when I have two fluid drops. If I squeeze
them together, I have to put an extra force on. And that force is proportional
to the Laplace pressure. The larger the Laplace pressure, the larger is that
force to squeeze them together. So an important consequence of the fact
that when you squeeze the drops together is that an emulsion can actually
become solid. This is a very interesting effect -- you're mixing two fluids,
you're mixing oil and water. Or for example, when Nandu made aioli, he
mixes water and olive oil with a little bit of egg -- that's a surfactant--, when
he mixes them together and he mixes them properly, when he emulsifies
them, he takes two fluids oil and water, and ends up with a solid.

Another very common example is mayonnaise. Mayonnaise is just oil,

water, and egg yolk. And we can understand why the emulsions become a
solid by understanding the fact that as you pack the drops together to a
larger and larger degree, as you pack them together, you have to deform the
interfaces. And that actually allows them to become solid.

Let's look at this. Here's a picture seen in a microscope of the aioli.

You can do the same thing with a mayonnaise. And you see that the drops
are all squeezed together. They're starting to deform one another. They're
packed in so tightly that they deform one another. So let's understand now
how this emulsion becomes a solid. How you mix two fluids together, you
make them into drops, and you change something that started out as a
liquid, and you make it into a solid.

So what happens is we increase the concentration of the drops, and

we decrease the drop side. We're making more and more drops a smaller
and smaller size, that's a larger surface area. We're making a larger surface
area of drops, we're storing more interfacial energy, we're putting energy
into the system as we mix them, but we're making a larger and larger
number of drops of oil in the water.

As you increase the number of drops in the water, as you emulsify

more and more of the oil in the water, you start creating spherical drops.
When the drops are far apart, they can remain spherical. But as you increase
the concentration, as you make them larger and larger, the concentration,
the drops have to start squeezing together.

And in fact, when you are above a certain concentration, that

concentration is something around 64% of oil in water. When you're above
that concentration, the drops can no longer pack as spheres. They have to
squeeze one another, just to be able to pack in. You can see this in this
image. As you put more and more drops in, you can't keep them spherical.
They have to start to squeeze together. And in order to squeeze together,
you're putting a force on the drops. Where's the force coming from? It's
coming from the fact that they're contained in the water. The water is
holding them together and squeezing them. And as you squeeze them, as
you put this force on, they become essentially a solid-like material. And that
is the origin of the solid-like behavior of an emulsion. You're squeezing the
drops so much, that they have to deform. You have to put a force on, and
they're trying to push themselves apart. They can't push themselves apart,
because they're held in place by the water. But the fact that you've squeezed
them, you've put this force on, actually makes them into a solid.

And what we have to calculate, we understand this it depends on the

concentration, the number of drops. And we parametrize the number of
drops as the volume fraction of the dispersed phase, the volume fraction of
the oil in the water. So we can calculate the total volume of oil, the total
volume of water. And the volume fraction is the volume fraction of oil divided
by the total volume, the volume of oil plus the volume of water. That's the
volume fraction of the dispersed phase. When that volume fraction reaches
this critical value, the value where the drops begin to deform one another,
then it becomes a solid. And then the emulsion turns from a fluid into a
solid.

At low concentrations of oil, when the volume fraction is less than

64%, then the emulsion will flow just as if it's water. It's water with just a
few drops of oil. But as I increase the oil, as I increase the volume fraction of
oil, then it becomes harder and harder to flow and ultimately, when it
reaches this value of 64%, it can no longer flow. It becomes a solid. So from
this, we can actually calculate what the elasticity is. First of all, we know that
it has to be zero, it cannot be elastic it's fluid, so it has to be zero below this
critical volume fraction. As the volume fraction increases, then the elasticity
also increases. In fact, it increases linearly, as shown in this graph. So above
this critical value it becomes elastic, and the elasticity increases linearly
above this. And this allows us to calculate what the elasticity of the emulsion
is. I show it here. It depends on the difference of the volume fraction
compared to the critical value. So the difference between the volume fraction
of an emulsion and the critical value. How much above that it increases
linearly. And the scale is set by the Laplace pressure. And so you can see, if
you look at this formula, as you increase the surface tension, you don't want
to decrease the surface energy, you want to increases it to get higher
elasticity.

Surfactants tend to decrease the surface tension. It doesn't matter,

they're stabilizing the drop. This small increase on the surface energy
doesn't really affect the elasticity. What's more dominant with elasticity is
the total area which is given by the size of the drops. So as you decrease the
size of the drops the elasticity increases. It goes inversely with the size of
the drop. Similarly, as you increase the volume of fraction above this critical
value, then the total elasticity increases. And this is shown by this formula,
which gives you the elasticity for an emulsion.

AVE WEITZ: Today we're going to talk about packing. And you can
understand packing in a very special way by thinking of these bubble gum
balls. They're spherical, and they pack a certain way. And you can see what I
mean when I pour them into this container.

When I pour them into this container, they fill the container to a
certain level. And there's a certain number of bubble gum balls inside of the
container. And what I'm going to tell you about works for candy, like the
bubble gum, but it works for any particles. It works for sugar. It works for
flour. It doesn't matter the size of the particles, it just matters that they're
not square in shape so they don't fill the whole volume. They fill only a
fraction of the volume. How much they fill depends on the way they pack.
And when you pour them in, they fill a certain volume. They fill a certain
fraction of the volume.

I can calculate that fraction in a simple way. I can measure the volume
of each of these spheres. 4/3 pi times the radius cubed, that's the volume of
each sphere. Then I can count the number of spheres and calculate the total
volume of the spheres. I can also measure the total volume of the container.
And we'll see that the volume of the spheres is less than the total volume of
the container. In fact, the fraction of the volume of the spheres over the total
volume, that's the fraction of volume that's occupied by spheres. And that's
called the volume fraction. And I'll quote that either as a fraction or as a
percent, a percent of 100.

So I know when I take spheres and I gently pour them the way I did
with these bubble gum balls, the spheres have to support themselves and
they occupy something like 58% to 60% of the total volume. That 0.58 to
0.6 is the volume fraction of these spheres. And that's determined, the
volume fraction is determined by the fact that each of the spheres must
support itself, must be supported by the number of neighbors that it has.

They're very disordered. And if I shake them gently [RATTLING], they

will actually start to pack better. And if they pack better, their volume
fraction increases. So the number per unit volumes goes up and the height
of the total number of spheres goes down.

They're packing more efficiently and the volume fraction is increasing.

And I know -- and this is calculated -- that if I have spherical particles, like
these bubble gum balls, the best I can pack them, if they're disordered, if
there's no relationship, between the position of one sphere and the next
sphere, then the best I can do is pack them to a volume fraction of 64%.
That's called random close packing. That's something that's still debated. We
don't know how to calculate that analytically. But every time we measure it
and every time we do a computer simulation, we get the same number 64%.

So spheres pack always to a maximum volume fraction of 64%. That's

the best we can do provided that there's no order in the structure of the
spheres. And we can only do that if we shake them until they reach this
maximum volume fraction. And that value depends only on the fact that
they're spherical. So we'll get exactly the same value if we use tiny spheres
or if we use huge spheres. We can only pack them to a volume fraction of
64%. It doesn't matter what the material is. It doesn't matter what the size
is.

However, if the particles are spherical, like these bubble gum balls,
then I can shake them even more. I can shake them very hard and the
volume fraction will increase even further. And the only way it can increase
even further is if they order. Each layer forms a flat layer and they order in a
hexagonal order. They order with this hexagonal packing. And the next layer
stacks exactly on the first layer. Now, they're ordered. They're no longer
disordered. They're ordered in a hexagonal packing. And when you do that,
and you measure the volume fraction, you see that it's gone up significantly.
Instead of 64%, which it was when they were randomly structured, when
they're ordered, when they're hexagonally ordered, their volume fraction,
increases to 74%. And this is not so surprising to you. If you go to a
supermarket and you look the way they stack oranges,, they'll pack them in
this very ordered array, and that's because they can, pack them more
regularly. It doesn't matter that they're not small like these bubble gum
balls. The big spheres will pack just the same way. And if you want to pack
them as efficiently as possible, with as high, a volume fraction as you can
get, you have to pack them in, this ordered array. And that's the way to get
the largest volume fraction possible. What's interesting about hexagonal
packing is that's something that's, very easy to calculate exactly. So we can
calculate that it's exactly 74%. This is different from the random packing
where we still can't do a, perfectly analytic calculation. When they're
ordered, we can calculate very simply exactly what the volume, fraction is.
So so far, I've talked about spheres. I've talked about these bubble gum
balls, which are absolutely, spherical in shape. What happens if the particles
aren't spherical?, After all, many things are not spherical. For example, here
are some M&Ms and they're not spherical. They're ellipsoidal in shape. How
do they pack?, What's very interesting is that although we think we
understand, everything there is about packing, only recently people have
measured, what the volume fraction of M&Ms are when you pack them.
They're very uniform M&Ms, but they're ellipsoidal in shape. They're no
longer spherical in shape. So if we measure what their volume fraction is and
we pour them out--, again, keeping them disordered. [POURING CANDY],
And we measure what the volume fraction of these particles is,, there's still
some space between them. But it turns out the space is greatly reduced.
And so M&Ms, ellipsoidal particles, pack much more, efficiently than spheres.
These pack to a volume fraction of 74%, quite a bit larger than the 64%,

that spheres packed when they were disordered. And this is something that's
only been discovered in the last few years, how, things like M&Ms pack. And
what's really surprising is that spheres are anomalous. They pack the least
densely of any shape. As soon as you move away from spherical particles,
they pack much, more efficiently. And so M&Ms pack to a much higher
volume fraction than do, the bubble gum balls. What about other shapes?,
Many things aren't as uniform as M&Ms or bubble gum balls. For example,
what about other candies, like these chocolate chips that, Michael likes so
much. How do they pack?, Let's see. [POURING CANDY], These are much
less uniform in shape. And if you look at them, you certainly see that they
can pack to a much, higher volume fraction than do spheres. But exactly
what volume fraction they pack to, I don't know. We would have to measure
it. If I look at it, I would say that they pack to a higher volume fraction than,
spheres, but not quite as high as do the M&Ms because these are not,
perfectly round or perfectly uniform in shape. The little point prevents them
from packing as uniformly as possible. But very generally, different shapes
will pack to, different volume fractions. And in all cases, if you shake them,
you get them to pack more efficiently. You get them to pack more efficiently
because they always have to be, supported by their neighbors but they can
find configurations where they can, fall into a more comfortable position
where they pack to a larger amount. It's very difficult to get to a lower
volume fraction so the volume fraction, always increases. And you can
always see that. If you take marbles, if you take spheres, if you take
anything and you, shake them, the level goes down, which means the
volume fraction increases. So if you want to pack efficiently as possible, you
shake them to get higher, volume fraction. That's why Michael, whenever
he's making chocolate chip cookies, he, shakes them to get as many
chocolate chips as he can into the cookies. So far, we've been talking about
particles, about candies that have, exactly the same size. Each candy has
the same size. But many times, the particles come in all different sizes. Well,
we can understand that too just by mixing different-sized chocolate, chips
together. So here, I'll pour in a few of the small ones. , And if I mix these
together [RATTLING], and I mix them enough so, that the big ones and the
small ones mix, then what I almost always find is, that the volume fraction
increases. And we can understand that in a very simple way. The big ones
have some space between them. And the small ones are so small that they

can fit into the smaller spaces. So if I have more and more different sizes of
particles, they can pack more, and more efficiently. So the volume fraction
will always increase when I have particles or, candies of different sizes.

DAVID WEITZ: So emulsions require there to be drops of one fluid in a

second. For example, aioli requires there to be drops of oil inside of the
water. Eventually, however, emulsions will fail. In fact, when Nandu made
the emulsions, he worried about their failure. When he made the hollandaise
sauce, he worried about it breaking. So let's understand a little bit about
what it means to have an emulsion fail. In order for an emulsion to fail, you
have to lose the drops of one fluid in, the second. So you have to lose the
drops of the oil in the water. And there are several ways that this can
happen.

The first thing that will happen is the fact that the oil and the water,
have a different density. Typically, the oil is lighter than the water.
Eventually, the oil will cream. The oil drops will come to the surface. This will
particularly be the case if the volume fraction is relatively low. The oil drops
come to the surface and in fact, pack and drain, and go to a much higher
volume fraction. You get a more solid-like emulsion at the surface. And
that's the beginning of one failure mechanism. Eventually, though, for the
emulsion to fully fail, the drops have to break, and have to recombine, so
you separate back into a continuous phase of oil on top and water on the
bottom for oil and water emulsion. You have to break the drops. And there
are several ways that this can occur.

The most obvious way is through coalescence. Two drops come close
to one another and they join together, and form a larger drop. Always, for
the failure of an emulsion, you have to lose the drops. And so the drops
have to become larger. It's the small drops that give the emulsion its
particular character.

So coalescence is one way. But there is another more pervasive way

that emulsions can fail and that is that drops can grow, and that is called
Oswald ripening. And that is absolutely pervasive. It's almost impossible to
completely eliminate Oswald ripening. Fortunately, it's a relatively slow
process. So it's not so important oftentimes, unless you store an emulsion
for a very long time. An Oswald ripening is the transfer of fluid from one
drop to another drop. And remember, drops are at a higher internal pressure
than the outside. And the pressure inside, the Laplace pressure, increases as
the drops gets smaller. So there's a driving force, an increase pressure to
drive the fluid, from the small drops into the large drops. The transfer of
fluid through the continuous phase between the drops occurs either because
the disperse phase is slightly soluble in the continuous phase. Or,
alternatively, it happens, because - remember, we talked about the micelles,
these aggregates of surfactant, where the core of the micelle is very oil-like
-- well, these micelles can swell slightly, can absorb some oil and can
transfer that oil across the continuous phase from one drop particularly a
small drop, where the pressure is very large, to another drop a large drop,
where the pressure is very low. So there's this driving force that drives the
fluid, drives the dispersed, phase from the small drops to the large drops. As
a result, the small drops get smaller, and the large drops get larger.
Eventually, the small drops disappear, and the large drops grow. And
remember, when you're trying to emulsify things, you're trying to make lots
and lots of small drops. And so the small drops disappear at the expense of
the large drop growing, that ultimately, leads to a failure of the emulsion.

So coalescence you can avoid with a proper choice of surfactant. But

with Oswald ripening, you have to avoid any transport of one fluid from one
drop to a second drop. You can do that by controlling the micelles and by
using a continuous phase that does not allow any of the dispersed phase to
dissolve in it. Oswald ripening takes a longer time and, typically, is not
what's the origin of the failure of an emulsion in foods.

So we saw how Nandu worried about the real failure of the emulsion.
He called it breaking the emulsion. And the reason that that's important is
that you're trying to disperse a very, very large volume fraction of the
dispersed phase in the continuous phase. So when you make aioli, for
example, you're trying to put a very large, amount of olive oil in the water.
And when he made hollandaise sauce, again, he's trying to disperse a lot of
butter in the water. And that gives the emulsion the thicker feel, the thicker
texture, and eventually, for example, for an aioli or a mayonnaise, it makes
it into a solid.

It's the large increase in the volume fraction. But because the volume
fraction of the dispersed phase is so much larger than in the continuous
phase, the emulsion can break. And what will happen is that it will, basically,
phase invert. The dispersed phase, which is the larger fraction, will become
continuous, and you'll get small drops of the continuous phase in the
dispersed phase. That's called breaking the emulsion. You get this phase
inversion.

And that's what Nandu was worried about. That's why he always has
excess water when he's making the hollandaise sauce, or when he makes
the aioli - he wants to avoid the breaking of the emulsion. In fact, when you
make aioli, you listen to the way the emulsion sounds, with a mortar and
pestle, particularly, if you're not using eggs, if you're making a true aioli. You
listen how it sounds. And as it becomes more and more concentrated in the
dispersed phase, as you emulsify more and more oil, then what Nandu will
do is add just a tiny amount of water, which is a tiny amount of the
continuous phase, to avoid the breakage of the emulsion. And that's the
primary type of failure for these emulsions.

HAROLD MCGEE: Hello. It's Harold McGee again. This week to talk with
you about emulsions and foams, which are different sorts of structures than
the viscous solutions that we talked about last week, but they have a similar
role in the kitchen. They structure flavorful liquids so that they flow slowly,
they cling to foods, they cling to our tongues and our palates, and prolong
our pleasure. They do that not by filling the liquid with long, tangly
molecules, but, instead by filling the liquid with pockets of air or of fat, which
also get in the way of water flowing easily from one place to another and,
therefore give a viscosity, a thickness, to the liquid.

Now to prevent the bubbles from collapsing or the fat in the droplets
from puddling together, we have to surround the bubbles and droplets with
stabilizing materials, which are often molecules like proteins. But it can also
sometimes be particles that collect at the interface between the liquid and
the air or the fat and help protect the bubbles or the fat droplets.

Foams are interesting because they kind of vanish in your mouth as

you pop all the bubbles. Think about the milk foam on a cappuccino or the
head on a beer. They have flavor, but then all of a sudden they disappear.
You can also make solid foams, which quickly collapse in your mouth to
release flavor and of course have an interesting, weird kind of texture.
Marshmallows do that. Meringues and souffles are other examples. And
those last two are made with eggs. And egg whites are really good at
making foams. They're 90% water, only 10% protein. But those proteins are
just very good at stabilizing bubbles. Not all proteins are. They're so good
that egg foams are used to provide aeration in cakes and other baked goods.
And cooks have known for hundreds of years about some tricks to make
really, good egg foams, foams that are as stable as possible and leak as little
liquid as possible so that they maintain their structure and give real,
lightness to the food that they're being added to.

It was one of those tricks that inspired me to do some of my first

experiments in the kitchen. And they were really important to me because
they taught me not to assume that scientists know more than cooks do.
Because what at first looked to me like an old cook's tale with no scientific
basis, turned out to be absolutely true and to have some really interesting
chemistry behind it.

So when I was writing on food and cooking back in the late 1970s, I
read in Julia Child's book, Mastering the Art of French Cooking, that if you're,
going to whip egg whites to make a meringue or a souffle, you should use a
copper bowl. She said that copper bowls acidify the egg whites and thereby
make them more stable and make the foam more stable. Well, this didn't
make sense to me chemically because metals don't change the acidity of
solutions. So I figured that there was really nothing to it. I did take a quick
look in the books about eggs that I had, didn't see anything about the
effects of metals on egg whites. And so I decided there was nothing to it and
didn't pay any further, attention to it.

But then later on, I came across a drawing from the 18th century, so
hundreds of years ago. It was a drawing of a pastry kitchen and the kinds of
things that take place in it. And the drawing came with a key. It was a
French pastry kitchen of course. And the drawing showed what looked like a
boy whipping egg whites in a bowl. There was whisking going on. And the
bowl was heavy, spherical, the way copper bowls are. That caught my eye.
And the key to the drawing said that in that particular part of the drawing, a
boy was whipping egg whites in a copper bowl to make biscuits. So it
specified that the bowl was made out of copper. And that made me rethink
what I'd thought about Julia Child's advice. If the French have been doing
this for hundreds of years, then maybe I should take a closer look.

So I went into my kitchen and did some controlled experiments. I

whipped egg whites in a glass bowl and a copper bowl side by side, which I
should have done long ago in the first place. And found that there was a
tremendous difference. They looked different. They had different textures.
Sure enough, the copper foam was much more stable than the glass foam. It
also took much longer to form than the other one. So there was clearly
something very interesting going on with copper bowls and egg whites. So I
found a sympathetic scientist with some instrumentation that would help us
figure out what was going on. He and I did some experiments and came up
with a theory that the copper was actually influencing one of the proteins in
the egg white, which was designed in fact by nature to bind metals and to
carry the metals around in the body of the developing chick. So we came up
with this theory. And we thought it explained what was going on, all the
different aspects of the phenomenon that we saw. And we wrote up a paper
and submitted it to the scientific journal Nature, which published it. So it was
a fantastic lesson for me in the kind of understanding that cooks, have
developed over the centuries simply by working with these materials, day in
and day out. And sometimes science has to catch up with the practical,
everyday understanding that practitioners have.

But one of the most delicious foams that we can make, I would say
much more delicious than egg white foams is whipped cream. Whipped
cream is a foam that is stabilized not by proteins, but by fat droplets.
Because cream is of course, high in fat. It's a concentrated emulsion. It's
about 30% or 40% fat. Milk, of course, is an emulsion too. Cream comes
from milk. But in milk, which is about 3.5% fat, the fat droplets are few and
far between. And so they can't do much to stabilize the foam. So milk
foams, like cappuccino foams, are actually stabilized by the milk proteins,
rather than the fat. Anyway, cream is really our gold standard for an
emulsified sauce. We use the term "creaminess" to describe exactly that
quality, the lingering lusciousness in the mouth, the balance between
substance and lightness, perfect smoothness.

Cooks have come up with lots of different emulsified sauces, which aim
for that gold standard of creaminess. And one of the most popular is
mayonnaise, which is made with vegetable oil. So you start out with a water
phase. You introduce into that water phase droplets of vegetable oil and
keep crowding that space with droplets until it develops viscosity and,
becomes creamy and even goes beyond creamy. It becomes almost a
semisolid version of cream.

To mayonnaise, you start with an egg yolk. And the egg yolk is what
supplies the stabilizing, materials for the oil droplets. Egg yolk is about half
water. And it already has fat droplets dispersed in it and a variety of
emulsifiers that helps stabilize those droplets. So you take that egg yolk and
you start adding a little bit of oil and you whisk. And you break the oil up
into tiny little droplets, which then get surrounded and stabilized by the egg
yolk proteins and by other molecules in the egg yolks that emulsify lecithin
especially. And then you repeat. You add a little bit more and you emulsify
and you repeat and repeat. And the mixture gets thicker and thicker as the
oil droplets fill up that volume of water. And then because it gets a little too
crowded, you add some lemon juice or some water to give more volume for
the oil droplets to collect in. And then you start repeating again. You
emulsify more oil into that space. And you end up with a water-based sauce
that's 80% or 90% vegetable oil. But it's all in the form of tiny droplets and
so it's not oily and greasy the way oil itself is, instead it's creamy.

Things can go wrong with mayonnaise making. You can add the oil too
fast and so you end up whisking more of the egg solution into the oil than
vice versa. And you end up making a reverse mayonnaise and the
mayonnaise breaks. All of a sudden instead of being creamy, it becomes oily
and greasy. Or if you add too much oil for the amount of water phase that
you have so that the droplets get too crowded and they end up pushing up
against each other, they'll end up fusing together and they'll separate into a
puddle.

Sometimes though you can make a perfectly good mayonnaise. You

can observe the correct technique and make a nice mayonnaise. And then
hours later, all of a sudden, it separates. It just kind of falls apart. That
happened to me when I started to make mayonnaise regularly, back decades
ago. And it used to drive me crazy. I like to make what's called a grand aioli,
which is a garlic mayonnaise that you serve with a variety of vegetables and
fish. And you just dip the vegetables and fish into the garlic-flavored
mayonnaise, and it's delicious. It's made with olive oil, comes from the
South of France.

And so I would make mayonnaises perfectly correctly with olive oil and
garlic. And hours later, often just before my guests were arriving to have
dinner, the sauce would disintegrate. And I'd have to start all over again.

So I did lots of experiments to try to figure out what was going on.
And what I figured out was that the garlic didn't have much to do with it. In
fact, it was the olive oil. If I used regular oil, regular vegetable oils like
canola or grapeseed oil, or sunflower oil or something like that, the
mayonnaises would be fine. But whenever I made it with olive oil, and
especially olive oil that had been, sitting around for a while, it was the one
that tended to break. And so I figured out that if I made the mayonnaise just
with refined oil, and then added a little bit of olive oil at the end just to give
it the olive oil flavor, it would be much more reliable.

Well, a few years after I figured that out, I visited Sicily. And I
mentioned this to the people I was visiting. And they immediately said, yes,
we make our mayonnaises here just with olive oil. And it happens to us all
the time too. And we just say the olive oil goes crazy. They use a verb
related to the Italian word "pazzo" which is, crazy, nuts, bonkers. They just
say the mayonnaise does that. And they just have no way to deal with it. It's
just the way the mayonnaise is. And you live with it. You shrug your
shoulders.

Well, when I heard that from them, I went and checked with some
emulsion experts to try to nail down what it was about olive oil that makes
mayonnaises unstable. And it's still not proven, but probably what's
happening is that some of the impurities in olive oil -- which is unrefined,
that makes it so complex and delicious and healthy compared to refined oils.
Some of those impurities are in the oil droplets, and they apparently move
to the surface of the oil droplets in the emulsion. And they end up pushing
the egg stabilizers off the surfaces of those droplets so that they're no longer
stabilized. The oil ends up pooling together. So olive oil mayos are like time
bombs. They're slowly ticking away toward their ultimate destruction.

So cooking failures aren't always the cook's fault. Your technique can
be perfect. But then some detail of the ingredients, maybe the very thing
that makes the ingredient delicious, can conspire against you. Anyway, those
crazy mayonnaises drove me crazy until I figured out what was going on. If
you enjoy making mayonnaise and you like the flavor of olive oil and the,
health benefits of olive oil, well, I hope I've saved you some frustration.

DAVID WEITZ:

A wonderful example of an emulsion is actually something that Carles

Tejedor made in his lecture on viscosity.

He took olive oil and turned it from a viscous liquid into an elastic
solid. And he did that by gellation. However, in order to gel olive oil, which
is a hydrophobic liquid, you have to somehow add a gelling agent. In Carles'
case, he used gelatin. The problem is that gelatin will not dissolve in olive

oil. Gelatin is hydrophilic. It dissolves in water, whereas olive oil is

hydrophobic. So you can't gel olive oil directly. So, instead, what Carles

did was he mixed in, first a mixture of water and different types of
sugar,

he heated it up on the stove to dissolve the sugar in the water, and

then

he gently whisked the olive oil with the sugar water. Gently whisking
them

made them mix, but not too strongly. But remember, oil and water
don't mix

directly. Instead, the only way for them to mix is to form an emulsion.
He

emulsified the olive oil in the water. He made drops of the oil in the
water.

And then he added gelatin. Now, the gelatin doesn't dissolve in the oil,
but rather, dissolves in the water. The water is a continuous phase, and the
gelatin dissolves in that. Then, when he cools it, the gelatin solidifies, it
forms a gel, but it forms a gel only in the continuous phase of the water. And
the drops of the olive

oil remain suspended within the water. And that way you get a solidlike

phase by gelling this emulsion. You gel the continuous phase to form

an

emulsion. That also stabilizes the drops of the olive oil, because they

can't

move together, they can coalesce.

However, what's even more interesting is the fact that if you were to

normally mix oil and water, as you do, for example, to make a salad
dressing, and you shake it up and make much smaller drops, you would see
that it would become rather white. It would be very strongly scattering, it
would be opaque. However, if you looked at the olive oil gummies, they
scattered a bit, but they were much more translucent. They weren't very
strongly scattering. And the reason for this is that the origin of the
opaqueness, the origin of the whiteness in an emulsion comes from the very
strong scattering.

You have many drops of olive oil in the water, you had lots and lots of

interfaces. These interfaces are between two liquids with different

indices

of refraction. The indices of refraction tells you how much scattering

you

see. The scattering is exactly the same reason that you see a
reflection of

yourself in a glass. That's because there's some refraction of light,

some

reflection of the light from the glass interface. It's exactly the same
thing

that leads to the strong scattering between the oil drops and the
water.

However, because the indices of refraction of the sugar water and the
oil are

much closer to one another, there's much less scattering. And the olive
oil

gummy is much more translucent, rather than opaque. And therefore,

it has a very different visual appearance.

FOAMS

DAVID WEITZ: Foams are very much like emulsions, but are different
because instead of having drops of a fluid inside a second fluid, they have
bubbles of air inside of a fluid. Nevertheless, you can have exactly the same
effect.

You can have a foam that is solid, you can have a foam that's liquidlike,

and it's a way of putting air bubbles inside of a fluid.

Of course, one of my favorite foams is the foam that you see on the
top of

a beer. Beer foam will last for different amounts of time. Guinness
would

last for a long time, Budweiser for a much shorter time, but still, the
head

on the top of a beer is just a foam. They're bubbles of air inside of the

continuous phase, which is the liquid from the beer.

Nandu also made foam. He made sea foam and carrot foam. In both
cases, he I essentially mixed in, or whisked in, air to make bubbles of air
inside of

the fluid. Another very good example that maybe you're familiar with,
I like

very, much is the foam on the top of a cappuccino. The milk foam. Milk
is

something that, just as it makes a wonderful emulsion, it can also

make an

excellent foam. And in order to stabilize the bubbles, to keep the

bubbles

from coalescing, from joining together, to make them stable, just as

you

had to have in the case of an emulsion, so too in the foam, you need a

surfactant.

In this case, the surfactant goes to the interface between the

continuous

phase which is a liquid, and the air. Another very, very good example
is

whipped cream, which can become a very thick solid, an elastic solid.

So the amazing thing about a foam is that you're mixing a fluid and a
gas.

A fluid wants to fill a bowl, sit at the bottom of a bowl, a gas wants

to expand everywhere. You mix them together and you make bubbles
of the

gas inside the fluid, and you can end up with something that is a solid.

It's just like an emulsion. You get exactly the same effect, and we can

understand it in exactly the same way. So foams, you need to put

many drops, many bubbles of a gas inside a fluid. You need to have them
stabilized by a surfactant. And the result is that you can avoid the drops
from destabilizing in exactly the same way that you have with an emulsion.
So the drops in a foam can destabilize either by coalescence, or by Ostwald
ripening. Both of them lead to coalescence just as they do with an emulsion.
Here, in the case of a foam, the drainage, the fact that you get the creaming
of the bubbles, the bubbles going to the top of the foam, is much more
severe than in the case of an emulsion, because the density difference
between air and any liquid is always much greater than the density
difference between two liquids. So the bubbles tend to cream, go to the top,
and therefore, destabilize in a foam much more easily.

In order to stabilize the foam, again, you must use a surfactant. In this
case, if you think of what Nandu did when he made the sea foam, he added
a surfactant. In that case the surfactant was lecithin. In the case of the
carrot foam, he didn't add a surfactant. He used the carrot itself, the
surfactants in the carrot itself, as its surfactant. But in both cases, you
absolutely must have a surfactant to keep the drops, to keep the bubbles

stable, to keep them from coalescing, and that's the key to having a
foam.

What Nandu did was he mixed the foam. He whisked in air to make the
foam. But there's a second way, a completely different way that you can
make a foam.

And you know that if you go to a coffee shop and they put foam on the
top

of your coffee, or whipped cream on the top of your coffee, they used
one

of these whipped cream makers. In that case, you make a foam in a

completely different manner. What you do is you take a compressed gas
-typically, you use nitrous oxide because nitrous oxide is very soluble,I n
things like milk - you mix the compressed gas with the milk under high
pressure. The gas at that point is of sufficiently large pressure that it's a
liquid. And the two liquids mix and essentially, make an emulsion, an
emulsion of the compressed gas, which acts like a fluid, in the continuous
phase which, say, is the milk. Then, when you spray it out on the top of your
coffee or on the top of your, drink the pressure decreases because you spray
it out of the can, it goes to the low pressure of the atmosphere, and the gas,
which is emulsified and formed at high pressure so is a liquid, expands and
forms small pockets of air or bubbles of air.

There are other ways of stabilizing a foam in addition to just

havingsurfactant and keeping the volume fractions high. You can also force
the continuous phase to become, rather than a fluid,to become elastic. The
way you can do something like that is to gel the continuous phase. That's a
very common way that chefs use to create, for example, desserts. A mousse
is a foam where the continuous phase has been gelled. You can add some
gelling agent to form it into a gel, or you can freeze it, or you can solidified it
like having something that's a fat and having air drops in a fat to solidify
it just by lowering the temperature.

But if you solidify the continuous phase, you can prevent the air
drops,from
creaming, and the foam from breaking. Here are some microscope images
where we look at the foam. You can see that there are bubbles of air inside
the fluid. Here's some pictures of a whipped cream. You can see the bubbles
of air inside the fluid very nicely in these microscope images.
Now, a foam can become elastic. And it has an elasticity that is exactly the
same as an emulsion. The formula, the description of the elasticity of the
foam is exactly the same as an emulsion. It cannot be solid until the bubbles

pack at such a high density that they must deform. The equation for the
foam becoming elastic is exactly the same as that for the emulsion. It
depends on the volume fraction, the difference of the volume fraction from
the critical volume fraction, and it depends on the surface tension of the
bubbles that are pulling them together, and the inverse of the radius. And
again, the bubble inside a foam has to have a LaPlace pressure. Its pressure
must be larger than what you would see if it weren't confined to the bubble.
The larger the pressure, the smaller the drop. As you make the bubbles
smaller, the LaPlace pressure goes up. As you make the bubbles smaller, the
elasticity of a foam goes up.
Colloids

DAVID WEITZ: There's one more type of dispersion that we need to

discuss. So far we've talked about foams, which are air bubbles in a fluid.
We've talked about emulsions, which are water drops in a fluid. We also can
have solid particles in a fluid. These are called colloids.

So a colloidal suspension is a suspension of small solid objects in the fluid.

It's just like an emulsion, but we place the liquid drops with solid particles.
It's just like a foam, but you replace the bubbles of gas with solid particles.
And colloidal suspensions, colloidal dispersions are also commonly used in
food.

One of my favorite examples is coffee. The black in coffee is made of

small black particles, or colloidal particles, of coffee that give the black color.
You can have other things, for example, a puree; potatoes are made
up of small particles that are ground up. They also can move and flow,
because they're small particles. So the role of a colloidal suspension is
to transport solid particles, but do it in a fluid. So even though the
particles, the black particles in coffee are solid, the coffee itself is like a fluid,
because it's predominantly the water in which the particles are suspended.

Colloidal particles can actually also act as a surfactant. Colloidal

particles like to exist at an interface between two fluids. Just like a
surfactant molecule and amphiphilic molecule exists at the interface between
oil and water and stabilizes that interface, so too can colloidal particles exist
at the interface and stabilize the interface of the two fluids. Or they can
stabilize the interface of a gas and a fluid. So when you have colloidal
particles acting to stabilize the interface, if it's an emulsion, we call it a
Pickering emulsion, after Pickering, who was the first person to recognize
that colloidal particles could act as surfactants, could sit at the interface, and
stabilize the interface. And their role, just like in the case of surfactants,
their role is to prevent two interfaces from coming and coalescing. It keeps
two interfaces apart. So if you have colloidal particles on the surface of
drops of an emulsion, then those drops won't coalesce, because the colloidal
particles will act to stabilize the drops to prevent coalescence.

DAVID WEITZ: An excellent example that encompasses all the types of

dispersions that we've talked about is ice cream. Ice cream is both a foam,
an emulsion, and colloidal particles.
So ice cream is a foam, because there are lots of bubbles of air inside of it.
It's an emulsion, because we make it out of milk. And milk itself is an
emulsion of fat drops in the milk. It's a colloidal suspension, because some
of these fat drops are solid-like objects, they're little solid fat drops, and
they sit at the interface of the bubbles of the air. And they stabilize the
bubbles of the air.
So ice cream is one of the tastiest examples of all the types of dispersions
there are. The stability of ice cream arises both because there are colloidal
particles or fat particles that stabilize the interface of the bubbles, but
also because in the continuous phase, the water phase is frozen, and it
becomes itself a solid. So the foam itself becomes solid, and that prevents
the motion of the drops of the air from coming to one another and
coalescing. In order to understand the ice cream better, let's look at some
images of ice cream. We can look and see the bubbles of ice cream directly,
if we look in a microscope. But a much better way to image the ice cream
into use an electron microscope. Then we can retain the full structure of the
ice cream, because we can take the images while it's cold, and we can see
all the details.

So here's an image of ice cream taken with an electron microscope.

And you
can see that it's a foam. You can see these bubbles of air. And if we look
more carefully, you see that there's globules of fat. These are the colloidal

particles that are stabilizing the interface of the bubbles. That's the

colloidal particles stabilizing the foam by sitting at the interface. You

can't actually see the emulsion, because the emulsion is the solid
continuous

phase. It's milk, and therefore, cream. It's an emulsion, because there
are

fat drops inside the milk. You don't see that in the microscope image,
but

you do see the fact that there are colloidal particles. the stability, the
stabilizing objects on the drops of air, which is the foam that makes

them

the ice cream.

So when you make ice cream, you cool it down, you whip it up, you
stir it,

so you mix in air to create the foam. And you freeze it, by mixing the
air,

by mixing it to make the bubbles of air, you also bring the particles to
the

interfaces of the bubbles. That stabilizes the bubble. And then you
freeze
it, you solidify it to change the continuous phase from water into a solid,

into ice, so it's a solid. And that stabilizes it. And that solid is, in

fact, a solid emulsion, because there are drops of fat inside the water,

which has become ice. And that's the emulsion part.

Materials:

Mortar & pestle

Second bowl (for collecting the egg white)

1 small pot to place the garlic

1 cutting board to chop garlic

1 knife to cut garlic

Ingredients:
1 egg yolk
olive oil (or any other type of oil)
salt & pepper
1 clove garlic
tsp mustard
Procedure:
1. Separate the egg yolk from the egg white.
2. Weigh the egg yolk and calculate its volume using the density given

on the worksheet.

3.

a. Peel the garlic, place in the pot with water and bring to a boil, then
drain the garlic and cool in cold water.

b. Chop the garlic into medium-sized pieces, place the pieces in the
mortar, and add 2g of salt.

c. Mash the garlic using the mortar and pestle. The garlic should
become a smooth paste.

d. Add the egg yolk and mix everything with the pestle. Go to step 6.

4.

a. Add the egg yolk and a teaspoon of mustard to the mortar and
mix with the pestle. Go to step 6.

6. Measure out about 30 ml of oil. When your mayonnaise is done you

want to be able to calculate how much olive oil you have added, so you will
have to measure the final volume and subtract it from this initial volume.

7. Drizzle oil very, very slowly into the bowl or mortar while
continuously whisking or grinding with the pestle.

8. Once the emulsion stabilizes (you should be able to hear a very loud
smacking sound and the emulsion should be stiff enough that it wont fall out
of the bowl easily if flipped upside down), measure the volume of the
remaining oil and calculate roughly how much oil you have used. Next, use
your measurement to calculate the volume fraction of the mayonnaise.
Record this

9. Add salt and freshly ground black pepper to taste

28/11/2013 13:09:00

Gelation is a phase transition that turns a liquid into a

solid by forming cross-links, and that you need a critical number of
cross-links for the solid to form.
PIA SORENSEN: And you will also know that cross-links can form by a
variety of different processes, both physical and chemical.

And we'll also use it to talk about spherification, where calcium ions do

random walks to basically get two alginate molecules together and

make

them stick.

Ceviche - Which is a wonderful dish in which the protons that are in

lemon juice or lime juice actually diffuse through the fish

to cause it to cook.
And by measuring carefully how the fish cooks, the rate that the fish
cooks, you can actually find something fundamental about how
protons move in water.

This week we will discuss Gelation, Diffusion and Spherification.

Gelation is a common phenomenon in cooking -- it occurrs when cooking an
egg, when making cheese, or when making Jell-O. We will start out the week
by understanding two types of gelation processes: gels caused by proteins
and by hydrocolloids, the latter often being referred to as "modernist
thickeners" since they are a common staple in modernist cuisine. Nathan
Myhrvold, the author of the six-volume book Modernist Cuisine will explain
why "cooking with chemicals" isn't necessarily as bad as it may sound,
and Jos Andrs will show us some of the remarkable creations that
modernist thickeners make possible.

In the latter part of the week we will discuss diffusion and random
walks, which are the scientific processes underlying gelation. All of these
concepts are perhaps the most lucidly summarized in spherification -- the
culinary techninque invented by Ferran Adria, and illustrated by Jos Andrs'
cooking Spherified Parmesan Eggs for us.

In the lab this week, we will study diffusion in common foods: we will
see how soy sauce is absorbed by a cooked egg white, and you will then see
how the diffusion of hydrogen ions is at the heart of cooking Ceviche.

One of the most important phase transitions that

occurs in cooking is gelation.
So gelation occurs in many of the things that you might cook every

day

and also occurs in some of the more esoteric types of cooking that we

will

talk about this week.

So when you cook an egg, you, as we've already described, take an

egg, which

at room temperature is a liquid, heat it up, and then it becomes a

solid.

And it turns out that that process is an example of gelation.

Another example of gelation is the making of Jell-O. So Jell-O comes in

a

box, right?

And you basically boil some water, pour the Jell-O mix in, put it in the

refrigerator to cool it down, and voila, out comes a gel.

That's another example of gelation.

So a third example of gelation that we will describe this week is called

spherification.

This is Ferran Adria's remarkable creation of a new way of creating

food

that has a very thin gel layer on the outside that you will learn about
in

this week's lectures.

So it turns out that all of these different phenomena, when looked at

from a physical perspective, are really very similar.

And if we take a phase diagram, for an egg, I mean, as we've already

described, the phase diagram has, on the x-axis, temperature.

And there's a critical temperature where the egg cooks or whatever.

It turns out that the unified way of thinking about all of these
phenomena

is to consider a phase diagram, where what's going on is that there's a

critical number of cross-links in the gel, and that is what I would now
like

to explain to you.

So the basic physics of this is the following.

What you should imagine is, is that you have polymers.

So polymers are long strands that are intermixed with each other.
And you imagine that you have a mesh work of these strands that are
basically interweaving each other.

It's like that you have a bowl-and so you can think, sort of at first, of the polymers as being like a
bowl of spaghetti.
So they're just strands that can slide by each other and whatnot.
So what you do when you form a gel is that you somehow stabilize the
cross-links between the strands.
The cross-links are the places where the strands overlap.
So we simply put in this picture little red markers.
You're going to think about this as glue that keeps the cross-links from
moving by each other.
And when you do that, you've changed what was initially a liquid,
because

the polymers could flow by each other, into a solid because

now it's really stuck.

And what's interesting about this solid is, as opposed to my hand or

your hand or a piece of wood, in this solid, only a very, very small part

of

the material actually are the molecules that are causing the solid
to hang together.
Most of it is actually liquid.
You don't have to put very much of these polymers and these crosslinkers

in it to basically to get the thing to form a solid.

This is an experiment that you can do with a bunch of your friends in

the

following fashion.

You can simply take your friends, and get a group of friends together,
and

everyone get together in a room and start walking around the room
behaving

like a liquid.

If you sort of randomly choose one of your neighbors to hold hands

with, if

you hold hands with your right hand and your left hand, if everyone is

holding hands, and you choose different neighbors, you don't hold

hands with the same neighbor, you hold hands with different
neighbors, then

what will happen is that you and your friends will have formed,
essentially,

the physical structure of a gel.

That is, you won't be able to move.

You'll be stuck.

And the cross-links are the hand holdings that you are doing.

So now, in an actual gel, that is, in a gel that we use when we cook,
be it

an egg or Jell-O or whatever else, there's some typical distance

between

the different cross-links.

These are sort of the distances between that the things

bind to each other.

And if we call that distance l, the length between the cross-links, we

can

then use the equation that we described last week, E equals kT over
l cubed, to basically find out what the elasticity of the gel is.

And so solids are characterized by their elasticities, as we've

discussed, and this basically gives you, quantitatively, the
elasticity of the gel.
So now, if we compare the different types of gels that there are when
cooking, spherification, cooking eggs, Jell-O, whereas from an abstract
level, these are all very similar.
They consist of polymers with cross-links holding the polymers to
each other.
There are different chemical ways.
There are different categories of how cross-links can form.
There are basically two categories.
And in what follows, we are going to describe each of them in turn.
In the first category, the polymers actually come from some protein
component of the food.
This is what happens with eggs.

The proteins unfold because of heating, and then they stick to each
other forming cross-links.
Whereas in the second category, there's some other binding agent that
you're adding, some type of glue, that causes the polymers to
stick to each other.
GELS MADE BY PROTEINS
Let's start with the egg.
So this is the phase diagram of an egg.

We've showed this to you many times.

As you increase the temperature, we've told you that there are
different

protein components that unfold and bind to each other to form the

cross-links.

So now, let's examine in a little bit more detail how this actually
happens.

So the egg white, let's just start and consider the egg white.

The egg white consists of a sea of proteins.

There are little molecules that are proteins, that are clumped together

into little clumps.

Each protein in solution is, when you put it in at room temperature in a

sort of compact clump, sort of folded together.
When you heat the egg, at some temperature what happens is the
protein unfolds and actually becomes more like a stringy polymer.
And what you actually have then in solution is a sea of different
polymers that are floating around.
Now, it turns out that these polymers are sticky.
That is once it unfolds, they're actually sticky.
And they stick to each other.
And it's the sticking to each other of the polymers that causes the
cross-links in the egg.

And that's the reason that an egg solidifies when you heat it.
The reason, by the way, that when you cool an egg it doesn't unstick

and

doesn't go back into a liquid is because these cross-links are so

strong that when you cool it back down, they don't break back and the
proteins don't unfold.
The process is essentially irreversible when you do it the way
that we tend to cook.
So the next question is why is it that proteins are sticky when they
unfold?

And to sort of understand this, we have to remember what proteins

are.

So proteins, you will recall, are polymers, which are

chains of amino acids.

So there are 20 different amino acids.

And a protein is composed of some sequence of different amino acids.

Depending on the protein, there will be a different sequence.

Now, amino acids have different properties.
This is a list of the 20 different amino acids that there are.
They have names that range from aspartic acid, to lysine, to
glutamine, and so on.

And each of these different amino acids has different chemical

properties.
But it also has different physical properties.
And there are two types of physical properties that we want to

focus on right now.

So it's now possible in the modern era to find out what sequence of
amino

acids corresponds to any protein.

So this is the sequence of amino acids that corresponds to chicken

ovalbumin.

Each of these letters refers to one of the amino acids that I just
discussed.

And that is the major component of egg whites.

Now, the amino acids have different properties.

And I would like to start by focusing on two of them because these are

in a

certain sense the most important for explaining why the different
proteins

stick to each other.

There are some amino acids which are called hydrophilic.

And there are others which are called hydrophobic.

So a hydrophilic amino acid is one that likes water. "Hydrophilic"

basically means that it likes water.

Whereas "hydrophobic," it's phobic of hydro, namely water,
doesn't like water.

So if you put hydrophilic amino acids in water, they're perfectly happy.

If you put hydrophobic amino acids in water, they're perfectly said.
They don't like being surrounded by water, but they have no choice.
And their goal in life is really to cover themselves as much as possible
so they don't have to come in contact with water.
Now, they also don't like hydrophilic amino acids because hydrophilic
amino

acids like water.

So essentially the deal is that if you have a protein which has a bunch
of

hydrophobic amino acids, what they will try to do is clump together

and

stay away from water as much as possible.

Whereas the hydrophilic amino acids are happy being near each other
and

being in the water.

So with this as context, this picture right here is a toy model

of a protein chain.

So this protein chain has on it black dots and white dots.

And for the sake of argument, let's say that the black dots are
hydrophobic.

So these are amino acids which don't like water.

Whereas the white dots are amino acids that do like water.

So if I show you the string, then the question is what's going to

happen to

the string?

Now, if the temperature is low so that the protein doesn't want to

jiggle

around, it will try to fold into a compact clump.

And it will do that by basically clumping all of the black dots, the

hydrophobic amino acids together, so they touch each other

where they're happy.

And it will also moved into the inside of the protein, where they're
away

from the surface and thus don't want to touch water.

You'll put all of the hydrophilic ones on the outside surface.

They can contact water.

And you shield the hydrophobic ones so that they don't touch the
water.

Now, of course, it's not possible to do this perfectly because they're

also

all attached to a string.

So you might end up with some hydrophobic bits on the surface.

But you try to minimize that as much as possible when you fold the
water.

And in fact, the principle of minimizing the free energy of the

protein leads to this configuration as the most favorable state when

you're

at low temperatures.

Now when you're at high temperatures, then actually the

entropy starts to matter.

And the protein unfolds.

It unfolds because it likes jiggling around.

Entropy, as we discussed before when we were describing phase

transitions,

competes with energy and causes the protein to unfold.

And once it does that, then all of these black hydrophobic amino acids

that were initially buried inside are exposed and open for business.

The business that they're in, of course, is sticking to other

hydrophobic amino acids.

And so what happens is that the different unfolded proteins bind to
each other causing cross-links, which is what forms the gel
when you cook an egg.
So we can see this in sort of toy models.
It's also possible to do simulations of full proteins unfolding.
And we just want to give you a little bit of dose of reality.
So this is a simulation that was done of a protein, of a real protein that
is unfolding.
And this is a molecular dynamic simulation that actually includes all
of the forces and other things that we understand that are going on.

So initially in its compact state, the protein has lots of helices in them
and sort of bends.
And these are characteristic structures that proteins tend to have.
And when you heat it up, you see that the bends and everything go
away and

the protein unfolds.

The hydrophobic residues are open for business, for sticking to others.

So heating isn't the only way to cook an egg.

And for that reason, it's interesting to think about other ways of, even

within this simple case of an egg, causing this protein unfolding and

sticking transition.

So if you look at recipes, it turns out there are two other ways of

actually causing transition in eggs.

One is by changing salt concentration.

By actually putting salt, that can affect the way that proteins fold.

And the other is by changing the pH.

And I want to start by demonstrating that in this simple recipe for a

poached egg.

So in this recipe for a poached egg, if you look at the recipe, what it
calls for is one tablespoon of vinegar and four very large eggs.
So before you cook the eggs, you actually pour vinegar in the water.
And then let the recipe says is really quite shocking for those of us

who

cook eggs on a regular basis, which is it tells you to boil them, but only
for two to three minutes, which is a very short cooking time.
And it claims that if you do that, that you still will be
able to cook the egg.
So it turns out that when you put vinegar in water, what you are
actually doing is changing the pH of the solution.
So you're changing the concentration of hydrogen ions in the solution.
And in fact, you're increasing it quite dramatically when you put
vinegar in the solutions.
So why does this make a difference?
So if we go back to the table of proteins and their properties, we so
far has emphasized that there are some proteins that are hydrophobic

and

others that are hydrophilic.

But there's one more important property that is worthy of mentioning,
which is that some of the amino acids have negative charges.
So aspartic acid and glutamic acid have negative electric charges,

whereas arginine and lysine have positive electric charges.

And electric charges, of course, are another way in which the amino

acids

on the protein can interact with each other.

So if we go back to our little picture of proteins from before, the

protein

had black dots and white dots, which referred to hydrophobic and

hydrophilic amino acids.

But some of the amino acids are also going to have electrical charges.

So some of them are going to have positive charges.

Some of them are going to have negative charges.

Now basically, the way that physics works is that like charges repel
each

other and unlike charges attract.

So if you put a positive charge next to another positive charge, that
causes a force that causes the thing to blow apart.
Whereas if you put negative charges next to a positive charge, they

like

to come together.
And there is in fact an electrostatic energy of the system which is
proportional to essentially the square of the charges, that contribute to

the

free energy of the protein in solution.

Now, of course, when the protein is folded up, it's already
compensated

for these charges.

And when you heat it up, it unfolds, compensating again for the
charges.

But it turns out that one thing that you can do to sort of manipulate
when

proteins fold and unfold is to actually change the charges of the

protein while they're in solution.

And the way to do that is to change the pH of the medium.

Because you see, it turns out that when we say that an amino acid is

charged, the charged amino acids change their charge depending on

the

pH that they're in.

And so what we can do is if we make the solution more acidic
therefore, we

can make the charges more dramatic than they were before.

And thus, the proteins become easier to unfold.

It is similarly the case that if we make the solution very basic, if we

actually make the pH closer to 14 and push it in the basic direction,

then

they also require a more dramatically different charge than

they would have otherwise.

So one simple way of seeing this in the context of cooking is that we

can

of a

make a plot that I will show you right here.

And for now, we're not going to tell you how to make this plot.
But this is a plot that can be made by taking the amino acid sequence

the

protein and having an understanding of the charged state of each of

amino
acids as a function of pH.
So what you do is you go into the amino acid sequence and you simply
count the number of positively charged amino acids there are, aspartic

or

glatamine acid, or negatively charged amino acids, histidine and the

like.

And then simply count the number that there are and take into
account their

pH dependence and thus calculate the dependence of the total charge

on the

protein as a function of the pH.

Here is the plot for fish myosin.

So this is an important component of fish, which is presumably

important

when cooking fish.

And what you see here is that at neutral pH the charge is some

intermediate value.

But when you make the solution highly acidic, that is say around 2, the

charged state of the protein goes up dramatically.

It goes up by several-fold.

And that, of course, makes the protein much more unstable and will
make it

much more likely to unfold.

So that makes it much more likely to undergo from the uncooked

transition

to the cooked transition that we're all familiar with when we cook fish.

So similar sorts of transitions occur when you cook an egg.

If you go to a very basic solution, for example by putting vinegar in

the

solution, the net charge on the protein goes up dramatically.

So this, of course, raises the question if you wanted to actually
manipulate the pH of the solution, then how would you do it?

And this is a table of different materials that one could imagine using
when cooking and with the typical values of pH that they have.
So water, of course, pure water has a pH of 7.
Vinegar, which is what we were using the poached recipe, has a pH
around

2.4 and lemon juice is around 2.2.

Gastric juice, which is the material in your stomach, that's highly

acidic,

that has a pH around 1.

On the more basic side, you could add toothpaste to the food that
you're

eating, that turns out has a pH of around 9.9.

Baking soda is a more common cooking ingredient.

It has the pH of around 8.4, and so on, and so forth.

Now, the thing is, and one of the challenges we manipulating the pH

while cooking, is that of course we don't just want to cause the

proteins

to unfold and coagulate.

We also don't want to mess up the taste.

And if any of you ever had a spoonful of vinegar, you will note that it

doesn't taste very good.

So when you're adding vinegar to your egg, for example, vinegar is

one of

the essential ingredients for cooking ricotta cheese, you have to make
sure

that you add only a little bit so that it doesn't affect the taste.

And this is sort of one of the balances that we have in cooking

between on the one hand, causing transitions by changing the acidity;

and on the other hand, causing them with temperature.

When we change the acidity, we also tend to affect taste.

NATHAN MYHRVOLD ON MODERNIST THICKENERS

One of the misconceptions around modernist cooking is this idea of

you cook with chemicals. People will often tell me, Nathan, don't you cook
with chemicals? I said yes, and with elements too. Of course everything is
made of elements. Everything is a chemical at some level. The exotic
sounding ingredients that we use in modernist cooking are really no different
in principle than the ingredients that we traditionally use. They just were
given fancier names or they come from different traditions.

Let's take an example of making a gel. The traditional way to do this is

with a gelatin. A gelatin is usually done these days by boiling pig skins.
There are some gelatin made by boiling fish skins. Now, that's a way to
make a gelatin. It's a wonderful substance. It's got a set of properties.
Meanwhile in Asia, there's a 1 000 year tradition of using seaweeds,
seaweeds like agar for making a gel, Calling it agar sounds unusual. Oh god,
I don't want that nonnatural natural thing. But let me tell you, it's just as
natural as gelatin or essentially anything else you do.

The same thing is true of any of the modernist ingredients, whether

they're things like xanthan gum or gellan gum. Those are both made by
fermenting bacteria. But then again, yogurt and vinegar are made by
fermenting bacteria and wine is made by fermenting with yeast. There's no
particular reason to draw a line and say oh, fermenting with the bacteria
that produce xanthan, that's bad. But somehow fermenting with yeast or
with bacteria and other kinds of cooking is good. They're the same kind of
thing. A huge number of the gums that we use in cooking are called gums
because they come from plant sap. A good example is acacia gum, which is
also called gum arabic. It comes from the Acacia tree. It's a tree that grows
actually all over the world, but particularly prevalent in Africa. That's where
they grow it. And you can see the gum exude out of the Acacia trees.

In fact, there's a bird called the Cory Bustard whose name in Afrikaans
and in several traditional African languages means the gum eater or the sap
sucker because it goes and it likes to eat that specific gum. Locust bean gum
sounds quite exotic, except it comes from the seed pods of the locust bean,
which is available in your health food store under the name carob. The seeds
contain the carob. But the seed pod contains the gum. There's also some
ingredients which are modified. For example, there's things called modified
starches.

Now, that sounds weird. Why would you modify a starch? But, of
course, we modify searches in many ways. We grind grain into flour. If we
want to have white bread or a white cake, we bleach that flour. There's a
whole set of processes around food. And there's one big difference between
modernist ingredients and traditional ingredients. Modernist ingredients are
provably safe. You can't say that about traditional stuff because of a doctrine
that the Food and Drug Administration calls GRAS, generally recognized as
safe. When you invent a new food ingredient or you say hey, I'm going to
have this new kind of refined fermented product called xanthan gum, people
who came up with that had to go through lots of hoops to prove it was
completely safe. Most other things in our diet, no one's ever done that set of
proof for.

In fact, there's many people who believe that if ordinary table sugar,
sucrose, tried to be approved, it wouldn't be. Now, that sounds weird. But, in
fact, once upon a time sucrose was something you could only get from an
apothecary shop. It was no different than any of these other things. Then
people figured out ways to make it cheaply and to make it from beet and
cane sugar. And it became this incredible phenomenon. Since we all love
sweet things, it became part of traditional cooking. But, of course, it can
cause problems with blood sugar and diabetes. And it can cause problems
with cavities in your teeth and a whole series of other health issues. It's not
clear that if you looked at it today, you'd actually get it approved. So when
people tell me, god, all this weird stuff, I'm uncertain about eating it. I say,
you actually have your concern misplaced. You should be worried about all
the other stuff you're eating that nobody's ever tested.

In Ireland was this beautiful town a little town called Carrigan. And in
the 1400s--we always hear about the stories of Ireland and famine came
and potatoes saved them from starvation. Well way before the potatoes
came from South America all the way toEurope and saved many Europeans
for a long time these guys in the town of Carrigan began eating those
seaweed as a way to precisely fight the famine. I'm mentioning the word
"Carrigan" because it's a city that we're going to be talking a little bit later
when we talk about two seaweeds two products that come out of seaweed-iota and kappa--that they are called carrageenans and comes from the town
of Carrigan.

JOS ANDRS: HISTORY OF GELLING AGENTS

So it's only to start to bring you perspective of these names because

you're going to be listening more about it. And those are some of the
carrageenans you see over here. I have them written there. They are from
the family of the red seaweed. And there are many names--Chondrus
Eucheuma Gigartina Gelidium Gracilaria. Those are different seaweed names
that probably you can go to bed tonight without meeting them. I don't think
your life is going to change. But it's OK to know that things have other
names-- more than gelatin and that's it. And that's what we are hopefully
going to try to achieve today. This is a bigger than gelatins themselves.

This is a--can you see? Do you think that this guy liked to eat or no?
These was Henry VIII. I never had the pleasure of meeting him but I
wouldn't mind because it seems like his banquets were quite something. And
I'm only mentioning him because they would have these amazing dinners
that they would make these calves feet kind of jellies that they would serve
in many different ways. To see already that this happened around 1481 to
1547--so late 15th century early 16th already gelatin dishes were being
served in royal palaces across Europe. I'm putting you this photo because
that's an important moment. 1658--this was they first recorded time we
have of the use of agar agar that probably by now is a word that you
recognize because agar agar you can see it in many places. You'll find agar
agar in Whole Foods more often than not if I'm not wrong.

Now it's 100% right? Organic and [INAUDIBLE]. And I've seen it. I've
seen it in the one I go in Washington DC and Wisconsin. Very important-1658 the first known use that we found in Japan. Even though they were
using it way before it's the first time that we found a recorded writing of its
usage--of agar-agar--almost four centuries ago.

HAROLD MCGEE: GELATION

Hello. This is Harold McGee back with you again. This week you're
taking a look at the physics of diffusion and gelation. And the particular
example you're going into in detail is spherification, a technique that Ferran
Adria, one of the instructors in the course, co-founders of the course, came
up with about 15 years ago. I thought I would talk with you a bit about gels
in general, because they are a favorite preparation of cooks and, in fact,
have been for a long, long time. I think that's because they're beautiful to
begin with. They're often transparent or translucent. You can color them. You
can make them into decorative shapes. And they are solids that liquefy when
we chew them and release flavor and give a delicious, wonderful consistency
and feeling on the tongue. Some examples, of course, include jello and
things like that, fruit jellies, candies like gummy bears and Turkish delight,
but also egg whites. And it's kind of amazing.

These structures are usually mostly water, often 90% water or even
more than that. And yet that water is immobilized in a network of long
molecules, the few percent of weight of the structure, so that the overall
structure is solid rather than liquid. And the water is held in that network of
long molecules a bit like the way a sponge holds water. There are cavities in
there. And the water stays in the cavities. Now, the word gel comes from an
ancient root meaning cold or frozen like ice. And gelato is another word with
that same root. And that makes a lot of sense, because it's the case that
gels start out as liquids. And then they become solid with cooking. And then
some of them turn liquid again as we eat them, especially gelatin gels. So
again, an everyday version of this is jello. The haute cuisine version is an
aspic.

Now, there are some foods that gel on their own just with very little
encouragement from us or very little manipulation. Egg whites are an
example of this. What happens there is that the egg white proteins are only
about 10% of the weight of the egg white, 90% water. And yet when we
heat the egg whites, those long but folded up proteins begin to unfold. And
when they unfold, they begin to cross-link with each other, form bonds with
each other, and form a network that can then hold these pockets of water
inside them. In the case of meat juices, if you take a piece of meat or fish
and cook them in such a way that you collect the juices that get squeezed
out during the cooking process, that juice generally contains long gelatin
molecules. And these, actually, don't form permanent bonds with each other
the way the egg proteins do. But they do form weak bonds with each other
as the liquid cools down and the proteins begin to move less violently. And
that's what allows the gel to solidify.

Then, in the case of fruit jellies, it takes a little more work to make
those. First, you cook the fruit. You extract, in this case, long pectin
molecules, not proteins. These are carbohydrates. And then a combination of
added sugar and often added acid encourages those pectin molecules to
cross-link as the liquid cools down. There also modifications of natural
pectins that causes that cross-linking to take place with calcium, so that you
don't need as much sugar. And that's how you can make low-carb jellies and
jams. Now, cooks have had fun with gels and jellies at least since medieval
times. And they've done some really inventive things over those hundreds
and hundreds of years. So of them would be right at home in the restaurants
of the creative chefs who are lecturing in this course. We see the first recipes
for gelatin jellies in manuscript recipe collections beginning around 1400.
And then in 1517, there was a banquet that Henry VIII gave in his palace at
Greenwich. And one of the people who was at that banquet wrote down a
few impressions of it. And here's what that person said.

Every imaginable sort of meat known in the kitchen was served and
fish in like manner. But the jellies of some 20 sorts perhaps surpassed
everything. They were made in the shape of castles and animals of various
descriptions, as beautiful and admirable as can be imagined. So that's 1517.
In 1600, we have a manuscript recipe that gives imitation eggs for the
Lenten season, which was a time of fasting. And you weren't allowed to have
animal foods, meats, or eggs, or anything like that. You could have fish,
however. And so there's a recipe for eggs for the Lenten season, in which
you scoop out the egg from an egg shell, two halves of eggshells. And you
fill those halves with a fish gelatin that has been used to thicken white
almond milk, so that it looks like the white of the egg. So you fill the two
halves of the eggshell with this white almond milk gel. You let it set. And
then you scoop a hollow into each of the two halves and fill the hollows with
another almond jelly that you've colored yellow with saffron.

So it looks like egg white and egg yolk in an egg shell. But in fact, it's
fish jelly and, therefore, OK for Lent. And then around 1750, someone set
down a recipe for an arranged plate of food on which you have a replica of a
fried egg with a white-colored jelly for the white and a yellow-colored jelly
for the yolk. But then you also have bacon made out of jelly. That is to say
strips of brown and pink and white jellies all to imitate the different parts of
the strip of streaky bacon all arranged on the plate so it looks as though you
have a plate of bacon and eggs. And they also had recipes for replicas of
playing cards, edible playing cards, made out of gelatin that were then
colored by hand very carefully. And it was in this same period that the jello
shot was invented. Although, back then, it was called a punch jelly. It was a
mixture of sugar and lemon juice and rum and brandy. And one of the
recipes for this kind of thing said you could make it as strong as you please.
So some tastes don't change.

A few years ago, a couple of performance artists in the UK revived this

British jelly tradition with a bunch of really impressive jellies, perhaps the
most impressive of them being a replica of St. Paul's Cathedral. So there's a
long history of interest in gelatin gels and a lot of very practical science to
figure out in all of this. How do you get a gel structure with enough strength
and stiffness to take on these various roles but that still have some give, so
that in your mouth they're not hard and unpleasantly chewy? How do you
have structure on the one hand but a nice wobbliness that melts in your
mouth at the same time? And in fact, that's one of the great things about
gelatin gels is that they melt at body temperature. That is to say the
temperature of your mouth, which does give them that very wonderful
melting quality. But that's also a disadvantage, because it means they're
more difficult to work with. And you can't really serve gelatin jellies when
they're warm.

You can, however, use other long molecules to make jellies. And one of
them is agar, which is a seaweed version of pectin. It's a structural
carbohydrate that you find in the seaweeds. And it's unusual in its remaining
solid at much higher temperatures than gelatin jellies. It'll stay solid, won't
melt until you get up to about 80 degrees Celsius. It's been used for a long
time in Asia in cooking. But we associate agar with Petri dishes in
microbiology labs for growing bacteria. And it turns out that's a really
interesting story. It's because a woman who knew about Asian agar jellied
foods told her scientist husband about them in late 1881. The scientist's
name was Walter Hesse. And he was working with the microbiologist pioneer
Robert Koch, K-O-C-H, who first isolated the specific microbes that cause
tuberculosis, diphtheria, plague, cholera, and a number of other diseases,
very important figure in the history of microbiology. His laboratory was using
gelatin jellies to grow the bacteria on. And the problem with gelatin jellies is
that they melt in hot weather. And also the gelatin molecules, those
proteins, could be digested by the microbes that they were trying to grow on
them, which meant that the jellies would just liquefy.

So Walter Hesse's wife, Fanny, who cooked at home but also worked in
the lab with her husband had learned about agar from her mother, who had
lived in Asia and had passed along to her daughter recipes for heatinsensitive puddings and jellies and so on. And so it was a cook, in fact, who
introduced agar to the scientific lab to the Petri dish. And the fact that it's
now coming back into the kitchen in the West, well, it's an indirect route. But
it's about time. Ferran Adria, one of the co-founders of this course, began to
experiment with agar and other materials like it in the 1990s, trying to find
new ways to make jellies with interesting properties. And he came up with a
wonderful idea of mixing agar and gelatin together to make a more complex
gel.

The physics of that's probably pretty interesting. And what that

allowed him to do was to make a transparent jelly that could be served
warm and that he could form into what looked like raviolis but raviolis that
are transparent, so that you can see the food on the inside. And the dishes
that he made with this combination are really beautiful. They're almost like a
setting of jewels on the plate. And it was Ferran, as I've already mentioned,
who came up with the idea of using different seaweed carbohydrate
alginates to do what has come to be called spherification. That is to say the
controlled formation of a gel by way, not of heat or by cooling, but by using
calcium to cross-link the carbohydrates, much as calcium is used to crosslink pectins in low-sugar jams. So there are many things you can do with
gelation and with gels in the kitchen and in the laboratory. And they may be
transparent, at least some of them. But there's still a lot in them to see and
explore.

SPHERIFICATION

So now we want to talk about the physics of spherification. How does

this remarkable recipe work? So let's remember the way that we start. So
we're going to take a ball of juice. Maybe it's mango juice. Maybe it's pea
juice. I'm particularly fond of crushed olive juice. And you take it, you put
some alginate into the juice, so that basically within it, if you could see the
molecules, there would these long strands of alginate molecules that are
floating throughout the juice. And those strands, as we've already stated,
are negatively charged, and because they're negatively charged, they
probably don't like each other very much and they just float around,
avoiding each other. You then take the ball of this stuff and you dunk it into
a calcium bath. The calcium ions are positively charged and they, through a
process that we will start to describe, move into this sphere that you have
and start to cross-link the gel. They start to cause the gel to stick to itself by
these positive cross-linkers that we've told you about. And you start to form
a thin layer of gel around the outside.

And what we now want to focus on is this process of how the calcium
ions move in. How they actually move to cause the gel to cross-link to make
this wonderful spherified substance. Now one of the most interesting things
about this is that it turns out that the physical process that governs the
motion of the calcium molecules really occurs throughout cooking, and
indeed, throughout your life in various ways once you understand what it is.

And so, I just want to start, before we explain the physics, just to draw
this analogy so that you can hopefully start to think about things in this way.
So on the next picture, what I want to do is show you a picture of a steak.
So this is a picture of a steak which has been browned very heavily on the
outside so it's got this nice, crisp browned flavor, whereas it was cooked sort
of rare, and so on the inside of the steak, it's not so well done. And of
course, in order for the steak to develop this brown layer, heat has to move
in from the grill, or the stove, or however it is that you're making it, and
transform the initially flaccid meat into a nice, crispy, brown layer. And that
brown layer, that is, the brown layer in steak is sort of physically analogous
to the gel layer that forms outside of a calcium bath. We will show you that
these occur through the same process and the same way of thinking, and
they basically illustrate a fundamental concept of cooking that we haven't
yet mentioned, but that we will now finally get to. Which is, that, when
you're cooking something, how long you cook it matters.

Now, you all know this from your experience, if you're cooking Nestle
Toll House chocolate chip cookies, as I like to cook, and you put them in the
oven, you better cook it, if you use the standard recipe, around 10, 11
minutes. If you cook it for four minutes, then the cookie dough will end up
being undercooked. If you could it too long, the thing will burn and you will
have not very good cookies. So the reason the time matters when you're
cooking chocolate chip cookies is, of course, because the heat has to
basically get into the cookie and cause the phase transitions that we've
talked about in the past. When you're spherifying something, time matters.

How long you leave the droplet of wonderful olive juice in the solution
bath matters, because that tells you how thick the gel layer will be around
the outside of the spherified substance. If you take the wonderful ball of
olive juice and you put it into the bath, and you go away and come back an
hour later, what will happen when you come back is you will have a solid gel
of olive juice. So that when you bite into it, instead of tasting the wonderful
olive as a liquid through your mouth, you'll have this sort of jelly, gooky
stuff. It won't actually have the right mouth feel in your mouth.

I mean the point of spherification was to make the gel layer so thin
that you didn't even notice it was there. And so, this is all a matter of just
time. How long you wait. If you take your steak and you put it in the over,
and you come back tomorrow, it will be cooked. It will just be burned
throughout the steak. That's not what you want. So the time matters. And
the physical process through which time matters turns out to be rather
universal in cooking. So before we describe the physics, I just want to go
through one other example to connect this to something else that we've
done in this course. So you'll remember that a couple of weeks ago we
talked about making ricotta cheese.

So we told you that make ricotta cheese, what you do is you take milk
and you heat it up to a temperature which is around 90 degrees or 95
degrees Celsius or so. And if you do that, and if you then add a little bit of
vinegar to it, then what happens is that the molecules that are in the milk
start to sort of come apart, and they coagulate and form cheese. Now that
process of coagulation is, of course, making, a gel, and so it won't surprise
you when we tell you that this is the same process that we've been talking
about up until now. It's a different type of gel than nanospherification, but
it's still a gel.

Now, when we're talking about making cheese, we had you all make a
phase diagram for cheese. You'll perhaps remember this wonderful phase
diagram. But what the phase diagram did is it plotted on the y-axis the pH of
the milk-vinegar mixture. And on the x-axis, we plotted the temperature.
And so if you go up to 90, 95 degrees or so, you only have to add a little bit
of vinegar. You have to only change the pH of the mixture slightly below 7.
So if milk without any acid added has a pH around 7, you add only a little bit
of vinegar, and that causes the coagulation which gives you cheese.

On the other hand, if you wanted to make cheese at room

temperature, we pointed out that you could still do it. What you do, though,
is instead of just a little bit of vinegar, you have to add, really, a lot of
vinegar. You have to change the pH substantially of milk to cause it to
coagulate. Indeed, as we told you at the time, that's the reason that if you
take your bottle of milk and you leave it on the countertop without
refrigeration, the bacteria will grow into the milk, producing acid, and cause
coagulation, which is not very appetizing, but it's the same phenomenon as
what happens from a physical point of view when you just pour vinegar into
the milk and cause coagulation.

Now, in reality, when you're cooking milk, the process through which
the vinegar, and therefore the change of pH, causes the milk proteins to
unfold and stick to each other or whatever it is they do, it's sort of more
complicated because the milk is moving around. But if we sort of do the
experiment in a very particular way, we can make it emulate exactly the
process that we're describing for spherification, and for cooking steak and
whatnot. And the way that we do this is as follows. So this is an idea of a
demo that was invented by Daniel Rosenberg. And what he basically
invented is the following thing. You take a microscope slide and you take a
drop of milk and you put it on the microscope slide. And then, next to the
drop of milk, you put a drop of vinegar. Then you put the cover slip on the
slide and you look at the milk under the microscope. And so here it is.

So the milk under the microscope, of course, the molecules, the fat
globules of the milk, which are what you can really see, are jiggling around
undergoing sort of random motions, which is what molecules in milk do. But
then, the vinegar is sort of traversing in from the side. And when the vinegar
hits the screen, that is, the part of the image that you can see, it causes the
milk to coagulate. It causes the proteins to unfold and stick to each other.
And you see that, because the molecules are no longer jiggling. You see that
it's stationary. And as time goes on, you can watch the movie and the region
over which the milk has been made stationary, that is, it's been made into
cheese, is growing with time. And that process, that is, the growing of this
sort of stationary cheese-like layer of the milk is, physically, exactly
analogous to what is happening in the alginate when it's cross-linked by that
calcium. It's exactly the same physical process. The vinegar is invading. It's
stopping the milk. It's unfolding the milk proteins and causing them to stick
to each other. In spherification, the calcium is invading, and it's causing the
alginate molecules to stick to each other.

And in both cases, it's essentially causing an immobilization which is

stopping and forming a gel. So spherification happens through this same
type of process. And so, if you look at this picture, this is a picture of our
droplet, and for me, today it's going to be olive juice. And inside of the
droplet there is alginate, and outside there is calcium. And initially, before
the calcium invades, if I just look at a very, very small part on the edge of
the droplet, what you see is a flat region where there's olive juice, alginate
molecules, and no calcium. And then on this side, we only have calcium. And
if we then let it go, once we dunk it in solution, the calcium ions will start
moving in and causing the gel to form. And this milk demo is really exactly
analogous to the process that occurs.

RANDOM WALK

The amazing thing is that the essential physical mechanism that

underlies all three of these processes turns out to be essentially exactly the
same when we looked at from the right perspective, and that physical
mechanism goes under the name of the random walk.

So the idea of the random walk, to my knowledge, was first introduced

into the scientific literature by a great statistician named Karl Pearson, who
wrote a letter to the journal Nature in 1905 in which he described to the
readers the process of a random walk. And he asked the readers if they
could please help him try to understand it. Now, the journal Nature was then
and is today one of the great scientific journals that exists. And in the early
1900s, it was apparently permissible for a great statistician to, instead of
proposing an answer, to ask a question. This is no longer allowed in the
modern era. But anyway, back to random walks. So Pearson described the
following process. He said, suppose that you have a person who has a coin,
and the person basically flips a coin. Like, for example, you can imagine I flip
a coin, and if the coin comes up heads, then what I'm supposed to do is take
a step to the right, and if the coin comes up tails, then I'm supposed to take
a step to the left. And what you're supposed to do is every second or so you
take the coin, you flip it, and if it's heads, you move to the right, and if it's
tails, you move to the left. And this process of randomly moving to the right
or the left Pearson called the random walk, and he asked the readers of the
journal Nature if anyone could help him try to understand the mathematics
that underlies this process.

Now, Pearson wrote this letter in 1905. It turns out that if he had
really been a careful reader of the literature, he would have realized that,
actually, this question had already been answered in the literature not once,
but twice by two different people in the years that preceded.

So I'm going to start by telling you the second person that answered
this question because this is a person that you've presumably all heard of. It
was a man. He was a young man at the time whose name was Albert
Einstein, who had previously considered the process of a random walk and in
a context which is actually quite amusing from the standpoint of a cooking
class. So Einstein wrote a paper in 1904. This was one of the three great
papers that he wrote in 1904. And this paper had the title, \On the
Movement of Small Particles Suspended in Stationary Liquids Required by
the Molecular Theory of Heat.\ So the title is so boring that many of you
probably fell asleep while I was reading it to you, when I was telling it to
you. And indeed, on the surface, the paper looks like it's very boring. But
what Einstein did in this paper was to ask himself the question, if you take
essentially a glass of milk, and you look at the fat globules in milk under the
microscope, the fat molecules move around because they're being buffeted
by the other smaller molecules that are in the milk. And Einstein asked
himself what the characteristics of this process would be. And if you think
about it, the process actually is really very much like, on an intuitive level,
the random walk. Namely, if I were a fat globule, and there were little
molecules to the right and to the left of me, then what's going to happen to
me is, is that sometimes the little molecules on the right of me will push me
to the left, and sometimes the molecules to the other side will push me to
the right. And I will, therefore, get pushed both directions. And where I get
pushed at any moment, well, it sort of depends on whether the molecules to
the left of me or to the right of me are more vigorous. And so this is really a
process which has a mechanism that is very much like the one that Pearson
described, and Einstein worked out the mathematics of this process.

We'll introduce you in a minute to the central formula in Einstein's

paper. But he worked out the mathematics of the process, and he used it,
basically, to do something, which was to him quite important. And I think to
us it's quite important too, which is he used the answer to this question to
try to calculate what the size of the little molecules must be that are doing
the buffeting of the big fat globule. So he actually was interested in
calculating the size of a molecule, which is something we've talked about
before in this class.

So Einstein, as I said, was the second person who answered Pearson's

question about the random walk. So the first person who answered it is
someone who you've probably not heard of. He was also a young man at the
time. His name was Louis Bachelier. And Louis Bachelier was a student of
Poincare, who was one of the great mathematicians at the time. And
Bachelier was interested in really a very different phenomena. Namely, he
was interested in the movement of stock prices. He wanted to make a
model, sort of a mathematical description for how stock prices change with
time. Now, some of you might be stock watchers. You pick your favorite
stock, and you watch its price change as a function of time. But I don't know
what your favorite stock is. I don't really have one, but suppose it were
Apple. So some days the price of Apple goes up. Some days it goes down.
The price is buffeted by random factors that are moving it up and down. And
on the surface of it, if you think about it, it sort of sounds like it's undergoing
also a random walk. I mean, some days it gets pushed up. Some day it gets
pushed down. And Bachelier's hypothesis was that this was how stock prices
move. Now, we now know that it's a bit more complicated, that is, how stock
prices move, than what Bachelier imagined. But nonetheless, the formula
that in his paper he invented, a mathematical description, which was really
identical to that that Einstein had invented, it also answered Pearson's
question. And it will also be of great use to us now in our description of the
random walk.

So why do we want to know about random walks? So remember what

I said. So a random walk, if I were to be a random walker, I would take my
coin, flip it. It it's heads, I move to the right. If it's tails, I move to the left.
And then what is going to happen is I'm going to flip it large numbers of
times. So I keep flipping my coins, and maybe I flip it 100 times. And now if
this were a bigger screen, you could watch me undergo this walk as I flip the
coin. And a reasonable question that you could ask, which is really the
central question of this subject, is how far did I make it? So if I flipped the
coin 100 times, how far from my initial position am I going to make?
Actually, the way, colloquially, in the literature and in the popular press,
people sort of think of the random walk as what they call the, drunkard's
walk because they think of it as the process that a drunkard might go in
when he or she walks down the street. So what does this have to do with
cooking?

What does this have to do with spherification, with cheese making, or

with heating a steak? So imagine that instead of a drunkard, that I am a
calcium molecule. And I am a calcium molecule which is going to participate
in the distinguished task of spherifying a ball of mango juice with alginate
polymer inside.

So you remember the set up. So the alginate is on this side, and I am
a calcium molecule, and I'm sitting over there. And what I would really like
to do, the great thing in my life would be if I could please go into the
alginate solution and cross-link two strands of alginate to start to make this
gel, this thin layer of gel that Ferran Adria created. So what would I do?
Well, I am being buffeted by the molecules on both sides of me. And so
every second, instead of flipping a coin, I'm going to get pushed one way or
the other way. Sometimes I'm going to get closer to the alginate modules,
which is where I would like to be, and sometimes I'm going to move the
other direction. And so if we ask how far do I move, or how far in general do
the calcium molecules that are surrounding this ball of mango juice inside,
how far do they move? Then the distance they move is the distance of that
of a random walk. And this is, of course, a critically important question
because that's the question. We know that if the calcium gets into the
alginate, it will cross-link it, and that is what is actually going to give us the
thickness of the layer of the shell. And this, of course, is the critical, most
important thing about alginate and about spherification. I mean, remember,
as Ferran describes it, the whole point is to encapsulate the liquid drop by
such a thin layer of gel that when you put it in your mouth you can't even
feel it's there. So we want the layer to be thin, but it can't be too thin
because otherwise it will fall apart.

Similarly, if you were cooking a steak, and you were trying to make a
very nice brown layer around the edge of the steak, one would like the
brown part to be just the right thickness. We don't want the whole thing to
be brown. We want the middle part to be maybe slightly rare. We want the
outside to be brown. And we would like the heat molecules to get in exactly
the right distance. And the question is, the critical central question is, how
thick, how far, does it happen to make it in? And that is the question that
both Bachelier and Einstein asked and answered, namely, how far do random
walkers tend to go?

So OK. Now, I'm going to just tell you the answer, and the answer is in
the form of an equation. This is an equation that Bachelier and Einstein
wrote down, and we hope to convince you that it's of extraordinary use
when thinking about cooking. And so I'm going to, without further ado, just
present it. Here it is. This is our equation. So what the equation says is that
L, which is the distance that the calcium molecules move, or the distance
that heat moves, or the distance that the vinegar diffuses through the
cheese, that L is equal to the square root of 4 times D times t. So 4, that's
the number 4. D is a number, which actually characterizes the random walk
process, and it's a material-dependent process. Scientists call it the diffusion
constant. It is the single number that characterizes the random walk. And t
is the amount of time elapsed. Now, if you express the diffusion constant in
units of centimeters squared per second, then t, the time, must be given in
seconds, and then the length that you get out is measured in centimeters.

So this equation is the equation that describes random walks. It

applies to calcium that's sort of helping to cross-link alginate. It applies to
vinegar that's helping to make cheese between two cover slips. It applies to
temperature that's trying to change the phase of meat when you're cooking
it. And this equation is our equation of the week this week. And so, as such,
you should all now pause your computers, and you should all clap.
[CLAPPING] So there it is. Because we should really admire it, and hopefully,
we'll make you learn to admire it.

Now, in order to make you admire it, of course, you should be a

critical, cynical audience, just like I am, for example, and we need to show
you that you can use it to do something useful. And so what I want to do
just to start our use of this formula is I want to try to use it to ask a very
important question. If you find yourself lucky enough to be able to spherify
something, which means that you have a source of alginate and calcium
chloride. Then what I want to ask is, how long should you, if you make a
beautiful droplet of mango juice, and you put alginate inside and put it into a
calcium chloride bath, then the question is, how long should you wait?
Should you let the droplet sit there before you take it out and have a
finished shell?

So in order to do this, I need to tell you what D is. I need to tell you
the diffusion constant. This is going to be the diffusion constant for calcium
that is in water. And it turns out that that number is about 8 times 10 to the
minus 10 meters squared per second. That's just a number that you're
given. And what we want to ask is, if we want the shell thickness, L, to be a
certain size, then how long should we wait? So let's suppose that we want a
millimeter-thick shell. Suppose that you decide that that's what you want. So
this is what we do. We take the equation L is equal to the square root of 4Dt.
We know L. We know D. And what we want to do is find t. So in order to do
that, we square both sides of the equation. L squared equals 4Dt, and we
then solve for t, the time that it takes to get a particular L. That t is t equals
L squared over 4D. And if we now take that formula, L squared over 4D, and
we plug in for both L and D, we will be able to calculate the time. So let's do
it. So we take L. We want L to be one millimeter. D I told you was 8 times 10
to the minus 10 meters squared per second. In order to make this work, we
have to express the millimeter, one millimeter, in terms of meters, so a
millimeter is 10 to the minus 3 meters. So what we have is L squared, that's
10 to the minus 3 squared, over 4 divided by D, which is 8 times 10 to the
minus 10. And if we then sort of work that out, what we find is that the time
that it takes is about 300 seconds, which is about five minutes.

So you should, if you want to get a millimeter-thick shell, and you put
the drop in, according to this you should wait about five minutes. And
indeed, if you look at the recipes-- actually, the recipes tend to want a
slightly thinner shell than a millimeter. But if you wanted a millimeter-thick
shell, then this is how long you would have to wait.

OSMOSIS

PIA SORENSEN: So random walks occur all over cooking in many

different ways. And soon, you are going to see a video by America's Test
Kitchen, where they're showing you how to make perfect coleslaw that
doesn't get watery. And they're going to tell you about osmosis. And the
whole reason that the recipe works is actually because of osmosis.

So before we see that segment, let me just explain a little bit about
what osmosis is. So the concept of osmosis is very similar to diffusion in a
lot of ways, and it builds on random walks, just like diffusion does. And so
just as we've talked about how, if you have calcium ions or water ions, that
have been in one part of a solution, they will kind of naturally wander about
and spread out through the solution.

The same concept kind of applies here, except the difference is that in
a lot of biological materials, in cell walls, there are membranes. And they're
usually semi-permeable, as we say. And semi-permeable means that water
can diffuse through naturally, whereas, other molecules cannot. And usually,
large molecules cannot diffuse through, or very charged molecules, such as
ions, cannot diffuse through.

So here is just a line indicating a cell wall. You can imagine that this is
the cell wall of the cabbage that you are soon going to see in America's Test
Kitchen's video. And so what Dan is going to show you is that we have the
cell wall, which, the cell has water on the inside. And on the outside, he's
going to add salt to the water. And so we have a high concentration of salt
within the water molecules on this side of the membrane. And so what's
going to happen, because of osmosis, is that the water over here is
randomly going to random walk into the side of the salt and try to kind of
dilute it so that you have a similar salt concentration on both sides.

So osmosis is the movement of the water molecules trying to

equilibrate the salt concentration on one side of the membrane to be similar
to that of the other. So the water molecules are going to move around
randomly. They're going to be crossing the membrane in both directions. But
when they find themselves on the side of the membrane that has a higher
salt concentration, they're going to have a higher probability of staying
there. And so you're going to have an increase of water flux towards the side
of the higher salt concentration.

So now in this video with America's Test Kitchen, you're going to see
how they apply this principle to make better coleslaw.

I've read about this before, but never tried it. Delicious! This is clearly
a great dish for hot summer days when it's just too darned hot to cook. My
Other Half noted that it qualified as more of an appetizer than a dinner, but I
think that was a knee-jerk reaction to the idea of a cold collation for dinner.
In fact we both came away well satisfied, and full.

In the interests of time I may write up these results and then try to do
another lab later. It seemed to me that the "cooked" layer went fairly quickly
from 1 mm to 2 mm, and at the end of the hour was stalled somewhere
between 2 and 3 mm. Was that because of poor measurement methods, bad
experimental design, dilution of the marinade? Or was it because, as the
outer layer cooks, the permeability changes and the diffusion rate
decreases? I think it's very plausible that permeability changes as the meat
cooks in the acid, but my test wasn't designed to show it. More experiments
to follow. Comments will be VERY welcome.

GELS MADE BY HYDROCOLLOIDS

The second way that cross-links can form in gels doesn't involve
proteins folding and unfolding. But this involves situations where there aren't
proteins around, that the polymers are made of carbohydrates, and we need
ways for the carbohydrates to stick to each other. And this occurs through
the use of a binding agent. So the most important example of this
phenomenon that we will discuss this week is spherification. This is the
beautiful creation of Ferran Adria, in which a small shell of gel is created
around a very, very delicious food. And I now want to describe to you how
that actually works, that is, what are the elements of that. And to do that,
let's just start with a recipe.

So here's a recipe for spherification, and this is a recipe for something

that Ferran calls spherical tea ravioli. It basically contains some sort of a tea
mixture inside, and then he forms a gel around the outside. And we'll talk
about the physics of how the outside of the gel was formed in a little bit, but
first let's just focus on what the ingredients are. So if you look at this
ingredient list, you will notice that there are two ingredients which seem a
little bit unusual. One is called sodium alginate, and that actually is in the
interior of the tea. And the second is called calcium chloride, which is
essentially a type of salt.

So sodium alginate is a polymer that basically comes from seaweed.

It's a carbohydrate. And that, it turns out, is the molecule that actually is the
essence of the gel in this material. So alginate consists of polymers. And it
turns out that those polymers, when they are in solution, are negatively
charged. So they have an electrical charge, and they're negative. And as you
all know, electrical charges that are negative repel each other. That is, they
won't stick to each other at all because negative charges don't like each
other. So the question that we have to ask ourselves is, can we make them
stick?

So the first clever idea that you might have to make them stick is that,
well, maybe we should add positive charges. And so then you would think to
yourself, well, where can I find positive charges in cooking? And certainly, a
good source of positive charges is table salt. So table salt is made out of
sodium chloride. If you pour it in solution, the sodium atom and the chlorine
atom will disassociate, and you'll have positive-charged sodium atoms and
negative-charged chlorine atoms. The negative-charged chlorine atoms, of
course, won't like the alginate either, but the positive charges are going to
stick to it and neutralize the negative charge.

So now, if you imagine it, we have this polymer. And on the polymer,
we have these negative charges, and now there are these little positive
charges that are sticking to it. And that's all great. So now the polymers like
each other more than they did before because they're not as negatively
charged, but they still don't stick to each other. So it didn't work. So it turns
out, though, that if we use a different type of salt-- instead of using sodium
salt, we use calcium salt. Then we can solve this problem and make it work.
And that is because calcium salt, the calcium ion actually has two positive
charges. It's doubly charged. So when the calcium ion sticks to the alginate
molecule, one of the positive charges will cancel out the negative charge,
but there's still a positive charge left. And that positive charge can then stick
to another alginate molecule, thus allowing the two molecules to stick to
each other.

So if you remember back to the little demonstration that we described

that you should all go home and do with your friends, where you hold hands
with one friend and another friend, this is the same sort of thing. The
calcium ion is essentially something that can hold hands with two friends.
And if the calcium ion holds hands with two different friends, it will bind
those friends to each other. And if the number of such cross-links becomes
high enough, you then create a gel. So this is a sort of simple but really, I
think, quite accurate view of what's going on when you add calcium salt to
alginate. This is a more chemically-detailed version of what's going on. You
see the alginate molecule has a chemical structure, and there are places
within it that the calcium molecule can bind, thus causing two alginate
polymers to stick to each other. It turns out if you look through recipes
involving what chefs call hydrocolloids, there are many different types of
hydrocolloids.

So alginate is the first one that we've seen, at least this week, that is a
bit different than the types of materials we usually cook with, at least I
usually cook with. But in fact, there's a whole list of different hydrocolloids
that can be used. Another example is a molecule called gellan. There's guar
gum. There's xanthan gum. There's a whole list of hydrocolloids, and these
hydrocolloids can all be used to make gels. And then they all have slightly
different properties, depending on what you're trying to make. And I'd just
like to highlight the properties of a couple of the other ones, just so that
when you start to look at recipes, as we hope you are, that the chefs in this
course are creating, you can try to distinguish what must be going on. So
one recipe that is really quite elegant is Heston Blumenthal's recipe for what
he calls hot and cold tea.

So in this recipe, what he does is he takes a cup of tea, and he then

draws a vertical line through the cup of tea. And on this side of the tea, he
has at one temperature, and on this side of the tea, he makes it another
temperature. And it is designed so that when you drink it, your tongue, half
of your tongue feels the hot temperature, and the other half of your tongue
feels the cold temperature. I've never tasted it myself, but it must be a very
interesting sensation. So if you think about how you would do that, what you
need to do is you need to make both sides a gel. They have to be solids
because otherwise they will be weak. They will mix with each other. But they
have to be solids which have the same elasticity at different temperatures.
And it turns out that the way that Heston Blumenthal was able to do that
was by using a material called gellan.

And that is a material that, basically, it's a carbohydrate in the same

way that alginate is. But if one goes and looks at how the cross-links are
made in gellan-- this is a subject of active research. Here, for example, is an
abstract of an article, a review article, that was recently published on the
gelation of gellan. And when you look at it carefully, what it shows is that the
mechanism for cross-linking gellan is actually much more like an egg. That
is, it's much more having to do with structural change, protein unfolding,
that sort of thing, than it is like the alginate example, where charge are
leading to cross-links. So gelatin is really quite similar.

If you look into the chemical details of gelatin and how the cross-links
form there-- I mean, of course, when you make Jello, you have to first heat
up the gelatin. That is a red flag that you must be unfolding something, and
then cross-links form. And so that's actually much more like an egg than
spherification. So the reason that there are so many different types of gels is
that, of course, one would like to be able to manipulate the formation of gels
and cross-linking in lots of different ways.

So another of my favorite examples, just to give you one more

example of this, is methyl cellulose. So one of Ferran's other creations was
hot ice cream. So the question here was, how could you make something
which had the same texture of ice cream but actually was a solid at a much
higher temperature, like 50 or 60 degrees Celsius? And what Ferran was able
to show was that, in fact, if you use methyl cellulose, which is a gel that has
a much higher melting temperature then gelatin and other gels like that, the
methyl cellulose could, if used in the right way, be used to make an ice
cream-like texture at an elevated temperature with a texture that is quite
similar to that of ice cream.

28/11/2013 13:09:00

So now we turn to our study of heat transfer. So heat

transfer is the application of heat to food. This is something that

you're all well aware is critical to cooking. And indeed, at the very
beginning of this class, when we defined cooking, we looked up in
the Oxford English Dictionary the definition of cooking. You recall
that the Oxford English Dictionary used heat in their definition of
what it meant to cook. They said that cooking is to make a food
fit for eating by causing a transition in phase that is typically
caused by heating. And so heating is very important.

So we now want to start to talk about the physics that goes

into heating food. Now, we've of course talked about this up until
this point before in this class. We've talked a lot about cooking an
egg. And we've sort of pointed out that when you put in a certain
amount of heat, an egg goes from being uncooked to cooked. And
this happens at a temperature, which depending on exactly how
you like your eggs, which is somewhere between 60 and 70
degrees Celsius. The perfect egg, you will recall, is at about 64
degrees Celsius. And we identified this as being near a transition
where some of the critical egg proteins unfold and then coagulate
with each other. So there were critical temperatures when we
cooked chocolate. We talked about the fact that chocolate has
five crystalline phases that have temperatures that range from 18
degrees Celsius to around 36 degrees Celsius and that the art of
tempering chocolate is hitting one of the crystalline phases and
making the chocolate be in that state, which is the state that our
mouths like the best in terms of texture.

So with that in mind, let's start to look at some recipes and

see how these heating protocols are actually implemented. And

the first recipe that I'd like you to look at is the recipe that
comprises the lab for this week of the course, which is one of our
favorite labs. In this lab, you will cook molten chocolate cake. So
molten chocolate cake, of course, is chocolate cake. But is not
completely cooked. The center is still molten. And so one of the
beauties of this recipe is that you'll see you'll cook part of the
cake but not all of it. And we will use that fact to study some of
the aspects of heat transfer during this week. So now let's look at
the recipe. So the recipe looks sort of much as you would expect.
It asks for chocolate, it asks for flour, it asks for butter, it asks for
sugar, it asks for salt. You put eggs in the chocolate cake. And
then, of course, once you've mixed all of these things together,
you put them in a ramekin or some sort of a container. And you
put them in the oven, and you're supposed to heat up the oven to
375 degrees Fahrenheit or about 190 degrees Celsius. That's
about 190 degrees Celsius. So we're heating up the cake to 190
degrees Celsius.

So let's then ask, what are the transitions that are occurring

in the cake? Well, it turns out that there are many different
transitions. All of them are not well understood. But the
transitions that occurred are within the range of 60 degrees to 80
degrees Celsius. Somewhere around 70, 80 degrees is where
there are transitions in the egg protein that help to give the cake
some of its solidity. Around 60 degrees is when the carbon
dioxide gas is emitted by reactions that we will discuss a little
later on in this course. But all of these temperatures are well
below the 190 degrees Celsius that we're actually putting the
cake in the oven. They're well below the boiling point of water, in
fact. And so this is a bit strange. Why is it that when we cook a
cake the target temperatures for the transitions that we want
within the cake are actually much lower than the temperature of
the oven in which we're putting the cake?

So you might ask yourself, scratch your head about this a

little bit, and say, well, maybe it's just that these guys who are
teaching this cooking class have given us a strange recipe. Maybe
they've given us a strange recipe, or maybe molten chocolate
cake is in itself a strange recipe. So why don't we just take a
moment and just look at the temperature heating protocols in
other recipes and compare them to the target temperatures that
one would like to produce within those foods and see how we do?
So here are some random examples. So this is an example of
meatloaf. So meatloaf of course consists of meet with other
ingredients-- tomato sauce and onions and whatnot-- all
packaged into a ball, and you're supposed to put it in the oven.
So the oven temperature for a typical meatloaf is about 350
degrees Fahrenheit or about 175 degrees Celsius-- so again, well
above the boiling point of water. So what are the temperatures
that are needed to cook the meat? Well, the temperatures that
are required to cook meat, it turns out, are also in the range of
50 to 70 degrees Celsius. In that range, there are proteins that
denature and coagulate. Collagen dissolves at a little bit higher
temperature but somewhere around 70 degrees.

But all of these temperatures are well below the boiling point

of water, despite the fact that when you put the cake in the oven,
you're putting in an oven which is at a much higher temperature.
So maybe it's just meat. Maybe meat is also strange. So here's a
recipe for cooking fish. This is a recipe for baking a tuna steak. So
a tuna steak, actually when you cook it, a good temperature to
cook it in, what a typical recipe calls for, is a little bit warmer than
that of the meatloaf, maybe around 450 degrees Fahrenheit,
which is about 230 degrees Celsius. So that's, again, much higher
than the boiling point of water. What are the transitions that
occur within tuna steak while it cooks? Well, it won't shock you I
hope at this point to know that those transition temperatures are
all much below the boiling point of water. Indeed, they're in the
range of 40 to 60 degrees Celsius, a bit lower than the same
transitions that occur when you're cooking beef, but still much
below the boiling point of water.

The reason that all of these temperatures are about in the

same range is not that hard to understand at the most qualitative

level. What's happening when you cook fish is also that the
proteins in the fish are unfolding. And they are coagulating with
each other. And that's what's causing the fish to cook. This is
what happens in fish. It happens in beef. It happens in most of
the things that we could cook. These are all biological tissues
which don't do very well, as you've perhaps noticed, when you
put them in boiling water. And so it makes sense to think that the
transitions would occur well below that. But yet the recipes call
for target temperatures in the oven which are well above the
boiling point of water. And this is really a mystery.

So why does this happen? So the answer to this is really at

the heart of why it is so difficult to heat food, to cook steak, to

make things by applying heat such that they taste good. And the
reason is really a very simple one once you understand it, which
is that it turns out that in order to properly cook something, it is
not sufficient to cook the inside of the thing you're trying to cook
to a target temperature. Like, you might want your steak to be
cooked around 60 degrees. It turns out you also have to have the
outside hit another target temperature. And that target
temperature of the outside is actually much higher than the
target temperature of the inside. It is even higher than the boiling
point of water. So to perfectly cook a fish or a steak or a meat
loaf, one needs to hit the outside of a temperature higher than
the boiling point of water, whereas the inside is at a temperature
which is much below the boiling point of water. And the essence
of this is why it's so hard to cook steaks, fish, other types of food.
So what we're going to do next is I'm going to explain what are
the chemical reactions that cause you to need such high
temperatures. And then we'll talk about heating protocols, which
try to achieve both temperatures at the same time.

BROWNING REACTIONS

MICHAEL BRENNER: So why is it necessary to cook the

outside of a

food to a temperature that's higher than the boiling point of

water?

That's crazy. So it turns out that there are a set of chemical

reactions which are perhaps the most important reactions in

cooking, at least if you like how your food tastes.

And these reactions are called the browning reactions.

So these are the reactions that tend to take food and make

ithave a brown color.

These reactions are called the Maillard reactions, after a

great

chemist, Louis Maillard, who, in the 19th century, discovered

and described them.

And it turns out that the way that these reactions work is

that they are

a reaction between a carbohydrate molecules, like a sugar,

for example,

and a protein, which could be a single amino acid.

And at high temperatures, which the target temperatures

tend to be well

above the boiling point of water, say around 120, 130

degrees Celsius, the

combination of a carbohydrate molecule and a protein will

lead to hundreds of small molecule byproducts.

Some of these byproducts are color compounds.

They tend to be brown, which is the reason food gets this

sort of brownish

color when it cooks.

But the other thing that this produces are flavor molecules.

These are small molecules which tend to have taste.

They're molecules that your tongue and the taste buds on

your tongue are able to sense and associate with rich tastes.

So one way to explain the importance of this, which at least

makes sense to

me-- we'll see if it makes sense to you-- is that when you

taste food,

when you taste beef--

I actually don't eat beef--

when you taste tofu, then there's this a very flavorful aspect

that one feels

in one's mouth when it tastes very good.

And you can't buy this flavor in the supermarket.

And you can go to the supermarket, and they sell spices or

they sell garlic,

they sell basil.

These have flavors.

But the type of rich flavor molecule that you taste on a well-

done grilled

vegetable isn't sold in the supermarket.

In fact, the only way to produce them is to actually induce

the browning

reactions on the surface of the food, which requires a

temperature that is

well above 120 degrees Celsius.

So as I said, these molecules that are produced from these

reactions are

small molecules.

They tend to be volatile, which basically means that when

you cook

them, they tend to go up into the air.

And so you can smell them if you're cooking something on

the stove and its

browning, then the small molecules that are produced that

are causing the

taste in your mouth also are going through the air.

And that's what you taste or you smell in your nose.

It's the same thing.

The same sorts of small molecules that cause smell also

cause taste.

And this is what you're trying to do with 120 degree or

higher temperature.

So if you then think about a steak or any piece of food-- so

here's a

picture of a steak-- so the outside is really quite brown.

There's a very thin crust, which is brown.

And that is where the browning reactions occur.

And then in the center of the steak, that's where you really

want this

perfect texture, the 60 degree perfectly done steak so that

it tastes very well.

And the challenge is sort of clear from looking at this cross

section of the steak.

On one hand, you want the browning reactions to occur on

the outside.

On the other hand, you want this perfect texture to

occur in the middle.

But given that temperature is a continuous variable--

so it has to go continuously from the edge to the middle--

how are you going

to make this work without messing up the food in between?

There are really various ways of doing this that chefs use.

So one is--and we discussed this before in this class-- is to

cook in a constant temperature heat bath.

So for example, you could, as Joan Roca showed us, take a

beautiful piece

of fish, seal it in plastic so that it doesn't lose the liquid

inside of it,

and dunk it in a constant temperature heat bath at whatever

temperature

you'd like your fish to be cooked at, let's say 60 degrees.

When it comes out, the fish will have a perfect texture.

But because the temperature is well below that of the

Maillard reactions,

there won't be any flavor molecules that are produced on it.

So if you were to taste it, it would taste really quite bland,

although it

has the perfect texture.

If you then take the fish and you sear it--

that is, you put it on a grill or on a very hot stove-- and you

sear it at a

very high temperature, you will produce the flavor molecules

in a very

thin layer.

And if you do it for a short enough time, the heat that you're

applying

won't mess up the perfect texture in the middle.

That's one way to cook a steak to basically get these

browning

reactions to occur.

Now, let's just think about this in a little more detail before

we move on

to next topic.

So how can we get a food to have a temperature above 100

degrees Celsius?

So you know and we've discussed before in this class that

the largest

ingredient in any food is water.

I am mostly water.

You are mostly water.

Your food is also mostly water.

And we've also told you, and in fact, you know from your

common experience

is that the highest temperature of the water can achieve is

100 degrees

Celsius, the boiling point of water.

The hottest it will get is it will boil.

But yet we want to heat up the food to 120 degrees Celsius.

So how can that possibly work?

If we put a steak or a piece of meat or a piece of fish into an

oven at a

temperature much higher than 100 degrees, the center of it,

where

there's lots of water, can't get higher than 100 degrees,

because it

can't go above the boiling point of water.

The only way that it can actually go above that temperature

is if you

actually boil off some of the water in the steak, the meat,

the vegetable,

the

whatever it is it your cooking, so there's a thin layer around

outside where it's actually dried out.

Once it's dried out, in that dried out layer, in that thin layer

which is

dry, you could push the temperature above 100 degrees

Celsius, and you can start to get close to the temperature that's
needed for browning reactions.

And that's the reason really that there's a thin crust of

brown around

food when you cook it, because these temperatures can only

be hit in the

part of the food where it's actually dried out.

Heat Transfer

Hello. It's Harold McGee with you again this week, and

talking this time about heat transfer, which, of course, is a

process that's at the heart a lot of cooking. Heat is energy of
motion, and by adding that energy to ingredients, we transform
them. We change them. We improve their flavor or texture or
both. At least we hope to improve them, but that doesn't always
happen. One of the most basic issues in cooking is controlling
heat transfer. That's especially important for protein foods like
meats and fish and eggs, dairy products, custards, things like
that, because the proteins are transformed at temperatures way
below the boiling point of water. And yet we're usually cooking at
the boiling point or even higher, and baking or frying or grilling.
Those high temperatures are good for developing flavor at the
surface of the food, and sometimes for drying it out and making it
nice and crisp.

But the question is how do you prevent that intense heat

from overcooking the inside?You overcook the inside, you end up

with tough, dry meat or fish or curdled custards-- nasty things.
There are a number of different solutions to this problem, and
cooks have been, of course, dealing with this for thousands of
years. One of the most traditional and at the same time
newfangled is cooking meats and fish in particular at very low
temperatures rather than high temperatures. That is to say, you
cook at just the temperature that you want the inside of the meat
or fish to reach, and that way, you simply can't overcook them.
It's impossible. And that's the basic principle of barbecue, low and
slow cooking, which is a very traditional and low tech method for
dealing with tough cuts of pork and beef that need long cooking
anyhow, and so you might as well do it at a low temperature.
That way, you retain more moisture.

Beginning around the year 2000-- so, very recently--

professional cooks started to use a technique called sous vide

cooking, which is new and high tech. It was first developed in
France in the 1970s, but it took a while to catch on in the rest of
the world. Sous vide means, in French, under vacuum, and it
involves, essentially, vacuum packing the food that you want to
cook and then taking that protected package and dipping it into a
water bath whose temperature is very carefully controlled with an
immersion circulator. So you can set it for any temperature you
want. The circulator keeps the water moving around, and you end
up cooking at a very precise temperature. Now, as I say, it's a
very new technique. It's made a tremendous difference, I think,
in the overall quality of the meat and fish that we get in and
restaurants these days. But it's true, I think, that cooks
throughout history have probably learned through their own
experience that low temperature meat cooking is a good idea.

Rotisserie cooking is an example of intermittent heat, which

turns out to average out into low temperature cooking. But the
guy who first demonstrated objectively that low temperature
meat cooking was a good idea did it not just a decade or two ago,
but two centuries ago. And I'd like to tell you that story, because
it shows how science isn't just a matter of specialized knowledge
about molecules or math, it's actually a way of thinking. Above
all, it's a way of thinking. It's about observing carefully, being
curious about what you see, noticing an interesting or unusual or
unexpected phenomenon, and then finding ways to understand
that phenomenon through controlled experiments-- coming up
with comparisons of different ways of doing things that teaches
you something about what's going on.

The man who first, to my knowledge, demonstrated the

importance of low temperature cooking was the man that I would

nominate for the father or founder of experimental kitchen
science, and he was a remarkable guy named Benjamin
Thompson, although mostly you find him talked about under the
name Count Rumford, and I'll explain that in a moment. Anyway,
he was active in the early part of the 19th century, and he
actually endowed a Rumford Professorship in Physics at Harvard
University. So Rumford, initially Benjamin Thompson, was the
personification of Yankee ingenuity-- a bit like Benjamin Franklin,
but with a few twists. So he was born in Massachusetts in 1753.
He had no formal schooling, but he married a rich widow and
ended up with a commission in the colonial militia as an officer
loyal to King George. So he picked the wrong side in the
Revolutionary War. And in fact, he commanded a cavalry outfit on
Long Island toward the end of the war, and his soldiers set up
camp in the local churchyard on Long Island. They used
tombstones to make the camp oven, and then they sent loaves of
bread to the locals with their deceased relatives' gravestone
inscriptions baked backwards into the crusts, which is kind of
horrific. I guess you'd call it something like psychoculinary
warfare.

So for obvious reasons, Rumford spent the rest of his life in

Europe. And he was a kind of expatriate Benjamin Franklin. He

began as a soldier of fortune. He began to work on the design of
cannons. That got him interested in heat, and he did several
experiments that cast doubt on the prevailing idea that heat was
a fluid. He suggested that it was a kind of vibration, and that
turns out to be close to what we understand heat to be today-that is, the energy of movement of atoms and molecules,
vibration included. Rumford also discovered, by the way, that the
movement of heat and liquids-- heat transfer and liquids-- is
mainly caused by convection-- the movement of the liquid's
molecules from one point to another. And he discovered that by
being curious about why it was he always burned himself when he
had a bowl full of thick soup.

What he found was that he would take a spoonful of the

soup from the top of the bowl, and it would be just the right
temperature. Then his spoon would go deeper into the bowl, and
the soup would be a lot hotter, and he'd end up burning his
tongue. He got to wondering why there was such a difference in
temperature between the surface and the interior of the bowl of
soup, and eventually worked out the fact that there was stuff in
the soup that was slowing the movement of the water from one
place to another. Rumford also became interested in heat related
household improvements, so he modernized the fireplace. You
can still see designs for the so-called Rumford fireplace. He
designed a coffee pot, which I think would still be an
improvement over a lot of coffee pots today. He came up with an
idea for a pot for dripping coffee which had a built in hot water
jacket, so that the coffee would stay hot, but it would never be
subjected to the direct heat of the stove, because he knew from
experience that direct heat from the stove destroyed the flavor of
the coffee. He also designed more healthful and efficient kitchens
in which fires were vented outside the house, and pots and pans
were insulated on the sides by recessed burners in the stove.

Anyhow, all this is prelude to the development that I want to

describe to you, which was his idea for a prototype of the modern
oven. That is to say, rather than cooking meats over an open fire
or over coals, he developed a metal box that was heated to
particular temperatures and in which the cooking was done. He
came up with that idea not directly, but very indirectly. It started
with his idea for a box in which he could dry potatoes. He wanted
to find a way to control the drying of potatoes so that they would
dry relatively quickly, but not get cooked. And so that meant
instead of warming the potatoes near a fire, putting them in a
box, and then heating the box very gently and in a controlled
way.

So he developed this potato dryer, and then, as he wrote in

an account just a couple of years after all this happened, he said,

"Desirous of finding out whether it would be possible to roast
meat in a machine I had contrived for drawing potatoes, I put a
shoulder of mutton into that potato dryer. And after attending to
the experiment three hours and finding that the meat showed no
signs of being done, I concluded that the heat was not sufficiently
intense. And despairing of success, I went home rather out of
humor at my ill success, and abandoned my shoulder of mutton
to the cook maids. It being late in the evening, and the cook
maids thinking, perhaps, that the meat would be as safe in the
drying machine as anywhere else, they left it there all night.
When they came back in the morning to take it away, intending to
cook it up for their lunch, they were much surprised to find it
already cooked. And not merely edible, but perfectly done. This
appeared to them the more miraculous as the fire under the
machine was quite gone out before they left the kitchen in the
evening go to bed, and they'd locked up the kitchen when they'd
left and taken away the key. So the leg of mutton had cooked
with no external heat applied. This wonderful shoulder of mutton
was immediately brought to me in triumph, and when I tasted the
meat, I was very much surprised indeed to find it very different
both in taste and flavor from any I had ever tasted. It was
perfectly tender, but though it was so much done-- that is to say,
cooked for so long-- it did not appear to be in the least insipid or
sodden. On the contrary, it was uncommonly savory and high
flavored. It was neither boiled nor roasted nor baked."

He notices this interesting result that if you cook a leg of

mutton at a low temperature for many, many hours, it ends up

being more delicious than it would be cooked traditionally over
the spit. Then he decided to take that observation a little further.
He then continues to write, "When meat is roasted in this
machine, its quantity determined by weight is considerably
greater than if it were roasted upon a spit before a fire."

To ascertain this fact, two legs of mutton taken from the

same carcass and made perfectly equal in weight before they

were cooked-- that is, setting up a good experiment-- these two
legs were roasted on the same day, the one in a roaster, the one
on the spit before the fire. And he's now calling his potato drying
machine the roaster. And to prevent all deception, the persons
employed in roasting them were not informed of the principal
design of the experiment. So it was a blind experiment. The
people doing the cooking didn't know what they were doing.
When these pieces of roasted meat came from the fire, they were
carefully weighed, when it appeared that the piece which had
been roasted in the roaster was heavier than the other by a
difference which was equal to 6%, or 6 pounds in 100. But this
even is not all. Nor is it, indeed, the most important result of the
experiment.

The two legs of mutton were brought upon table at the same

time, and a large and perfectly unprejudiced company was

assembled to eat them. They were both declared to be very good,
but a decided preference was given unanimously to that which
had been roasted in the roaster. It was much more juicy, and was
thought better tasted. As far as I know, this is the first formal
taste test in the history of the world. Anyway, both legs were
fairly eaten up, nothing remaining of either of them that was
edible. Their fragments, which had been carefully preserved,
being now collected and placed in their separate dishes, it was a
comparison of these fragments which afforded the most striking
proof of the relative merit of these two methods of roasting meat.
Of the leg of mutton which had been roasted in the roaster,
hardly anything visible remained except the bare bone, while a
considerable heap was formed of scraps not edible which
remained of that roasted on the spit.

Well, all this work on a domestic economy, on doing things

better in the kitchen, together with his work on cannons and heat
and so on, brought Benjamin Thomson a knighthood in the Holy
Roman Empire. Hence, Count Rumford. It also brought him a
great deal of celebrity and also wealth. Some of that wealth he
used to found the Royal Institution of Great Britain, which is a
museum of technology that still offers public lectures and
courses, some of them on the science of cooking. Some of that
money he turned out to leave to Harvard University for a named
professorship in physics. The current Rumford Professor of
Physics at Harvard University studies radiation physics, which is, I
suppose, a kind of cooking-- the cooking of matter that is not
terribly edible. But I think it would be fitting if one day the
Rumford Professorship at Harvard went to a specialist in the soft
matter physics of cooking.

28/11/2013 13:09:00
This experiment demonstrates heat transfer and
corresponding heat transitions in food. We've learned that food
cooks at much lower temperatures than that at which the recipe
calls for, why is this?

Well, it turns out that heat transfers from the outside to the

inside of the cake, and so the outside temperature needs to be

higher than the inside temperature but such that the phase
transition of the chocolate inside does not 'cook' and solidify but
instead remains in a liquid or semi-liquid phase.

To understand the heat transfer in this recipe, I used a hand

held food thermometer to measure the different temperatures of

a small cake at different locations (outside, inside and inbetween) and at different cooking times. So the variables in this
experiment were: time and temperature location inside the
cakes. The constant temperatures were: the same ingredients
for all the small cakes and the oven temperature. The response
variables were: how good the outside crust looked, and the
degree of 'softness' or 'liquidity' (?) or phase of the chocolate
inside the cakes. Then a diffusion coefficient can be calculated

It was difficult to measure the temperature at the different

locations inside the cake because the cakes were small and the
thermometer I used is not an instant temperature thermometer
type, but still I was able to obtain enough information and
variance in the data to calculate the diffusion coefficient and to
determine the 'optimum' cooking time to get the chocolate to
stay molten inside the cake.
Steamed

28/11/2013 13:09:00

Fermentation

Nathan Myhrvold: Time and Temperature in Cooking

Cooking is about using heat to create chemical reactions in

food. Cooked food isn't just hot food. It's fundamentally different.
If you cook something, and you put in the fridge and make it
cold, it's still cooked. It's just cold, now. It doesn't go back to its
same state. Whereas if you take a piece of metal, make it hot,
cool it down, it's pretty much the same as it was before. There's
an irreversible chemical change. Now, chemistry teaches us that
chemical changes usually require both time and temperature. And
the rate at which a chemical reaction will occur is some function
of time and temperature. Broadly speaking, there's a whole set of
foods for which the chemical reactions we call cooking happened
very fast. So fast, that pretty much the instant you reach a
temperature, it's done. Now, if it's not at that temperature, it may
not be done yet. But doneness means bring to a temperature,
and then you're done. That's it.

There's another set of foods where the chemical reactions

are fundamentally much more slow. And in those slow reactions,

we have to hold the food at a particular temperature for a period
of time. Most foods that are in the fast group would include fruits,
vegetables, eggs, and fish, and tender meats. If you are cooking
a filet mignon, as soon as it reaches a certain temperature, it's
done. For me, I like rare, about 120 degrees Fahrenheit. I like
medium rare to be about 130 degrees Fahrenheit. And so the
minute, the second, the actually tiny fraction of a second that it
reaches 130, it's done.

But tough meats are fundamentally different. Tough meats--

that would be cuts like brisket, like short ribs, like skirt steak-any of these tough cuts of beef, or of any other meat, for that
matter. Even though stewing chickens, or the leg meat of grounddwelling birds like ducks or pheasants. That tough meat is tough
because it has something called collagen in it. Now, collagen is a
topic totally unto itself, but for our purposes here, the thing that's
different about cooking these tough meats is that we have to
cook them long enough to soften that collagen. In traditional
cooking, that usually means cooking a stew or a braise. And
typical stew or braise, you might cook for an hour, two hours,
three hours, even overnight in some cases. And that's what
traditional cooking was about. It was about saying let's cook this
stuff very slowly, but at moderately high temperature. As a result,
braised or stewed meat tends to be gray. It tends to be dry
because that high temperature, also because of collagen, winds
up wringing the meat out from the inside out.

With sous-vide cooking, we can cook at a precise

temperature for as long as we like. And we can actually cheat this

collagen curve. We can get a rare or medium rare-like meat that's
still nice and red, it's still nice and juicy, but still degrade the
collagen, and make that meat tender. But to do that, we have to
extend our cooking times very long. That's because most
chemical reactions follow what's called Arrhenius's Law, or
Arrhenius' First Law of Chemical Reactions, that they are
exponential in temperature. So that means that the more you
increase the temperature, the faster they go at a dramatic rate.
With most food chemical reactions, if you drop the temperature
by 10 degrees you increase the cooking time by a factor of 10 to
get the same results, if it's in this slow set of cooking around
collagen.

As a result we will do sous-vide cooking for 24, 48, 72, or

even in one example-- oxtail recipe we have in Modernist

Cuisine-- 100 hours. Now, that requires a little planning ahead.
You don't come home from work and say, hey hon, let's have
hundred-hour oxtail. You kind of have to plan that in advance.
The interesting thing is by cooking that oxtail for a hundred
hours, or short rib for 72 hours, or pork ribs for 48 hours, you get
a texture that is totally unlike what you would get from braising.
Its delicious. It's unexpected. It's a way to take a meat and
reinvent it as something entirely new. And use something that's
both got a lot of flavor in it, and it's usually pretty cheap because
we generally price meats according to how tender they are.

Enzymatic Reactions Intro

So when we talk about fermentation reactions in yeast or in

bacteria, all of this is due to enzymes. So its enzymes that's

converting the large macromolecules into small molecules. And
none of these reactions could happen if they were just sitting
around at room temperature. The same is true in our bodies.
When we eat food and we break down the large food
macromolecules into small ones and we get energy in the
process, this could not happen at room temperature or the
temperature of our bodies. And so we need enzymes to speed up
this process. Enzymes are proteins, which means that a lot of
what we already know and have learned about proteins is also
true for enzymes. But enzymes are very special proteins. And
we're going to learn more about that in this segment.

So, for example, some of you may be lactose intolerant. And

what this means is that you have a lack or a deficiency in the
enzyme that converts lactose to its energy sources and breaks it
down. And this protein is called lactase. And in fact, many
enzymes end in the ending "ase" so lactase, protease, peptidase,
and so on. So when you are lactose intolerant, you can take a pill
that contains lactase. If you take this just before eating a dairy
product, this will help you break down the lactose and you're
basically taking care of the problem artificially. So what enzymes
do is they make chemical reactions happen faster than they
otherwise would. So if sucrose were just sitting around at room
temperature, it may eventually break down to fructose and
glucose. But in order to speed this up, there are enzymes that
basically cut those bonds and make it happen faster.

Enzymes speed up reactions either by helping to break

bonds or by helping to make bonds form. And in both cases,

enzymes often work by binding to the molecule or molecules in
question. And in terms of the bond breaking, they will then
facilitate this bond breaking happening faster by rearranging the
molecule, or by affecting the atoms in the molecules in some way.
In terms of making bonds form, enzymes do this in a simplified
way by bonding to two molecules and bringing them closer in
proximity. And this bond can then form more easily, because the
molecules are positioned in a way that make the bond happen
more easily. As so you can understand from this then that the
enzymes need to be very specially designed to fit the particular
molecules they work on. And so for each type of chemical
reaction that an enzyme catalyzes, it is designed to help that
reaction. And so it is the three-dimensional structure of the
enzyme that is important for binding to the molecules and for
causing the reaction to happen. And so if this three-dimensional
structure is broken or messed up in some way, you can imagine
that the enzymatic reaction would not happen.

Another way to think about this is in terms of activation

energy. So the energy that is needed to either bring molecules

together and make a bond form, or the energy that's needed to
make the bond break, that is the energy we need to put in to
make the reaction happen. And this is the activation energy, or
the activation barrier. In the review materials of this course, we
talked about how you can basically write out a chemical reaction
on a diagram where you show that the reactants go to products.
And we showed you how there's this hill in energy. And so the
energy needed to bring the reactants to their products needs an
input of energy. And this is the activation energy, or the
activation barrier. And so enzymes work by basically lowering this
barrier. So you can imagine then that the products would form
more easily, and the rate of the reaction would increase. Enzymes
are important for food and for cooking in many ways, and in fact,
in many ways that we may not think of normally.

So for example, when making cheese, the enzyme rennin is

what's causing the casein molecules to lose their negative charge

which makes them fall apart. And this causes the coagulation of
the case in which then leads to cheese forming.

Similarly, when fruit or vegetables are brown, this is also

due to enzymes. So what happens when you bite or when you

slice into fruit or vegetables is that these enzymes that were in
special compartments of the cell are then released, and they can
react with other compounds in the fruit or vegetable. So
America's Test Kitchen will tell you in their video about how to
make pesto. They will tell you about how this happens when we
slice garlic, and the flavor molecules are released as a result. Or
when we cut up onion, and this leads to reactions that cause
these very strong compounds that causes our eyes to tear.

In the case of browning fruit, the enzyme that causes the

browning is in a separate place compared to phenolic compounds.

And when you bite into a fruit or you bite into an apple, what
happens is that these enzymes react with the phenolic
compounds. Originally the phenolic compounds were supposed to
react with attacking insects or animals. But the browning
enzymes then react with these compounds and this causes,
together with oxygen, these large brown compounds. And this is
what we see when we let an apple, or a banana, or avocado just
sitting out on a counter for some time.

Since enzymes are proteins, they are going to react in many

ways just the same way that proteins do. So for example, when
we apply heat to enzymes, they're going to denature and
recoagulate just like the proteins did when we talked about
cooking meat in the heat transfer week. Similarly, when we
discussed ceviche and adding vinegar or lemon juice to fish and
this caused the proteins to denature, this is a similar way that
enzymes will react if we lower the pH and, hence, change their
internal structure in some way. This is actually something we can
use when cooking.

So for example, the enzymes bromelain and papain are

enzymes from pineapple and papaya. And these are often found
in meat tenderizers, because they break down the proteins. And
so that makes the meat more tender. Now, if you've ever tried to
cook pineapple jelly, the recipe probably told you to heat the
pineapple in some way before adding the gelatin. And this is
because if you don't do this, the bromelain enzyme will actually
break down the gelatin, and so the gelatin will not form the jelly
that we want when making the fruit jelly. Similarly, America's Test
Kitchen will show you that if you add an acid, lemon juice or
ascorbic acid, when making pesto, this will keep that green color
of the pesto, rather than have it turn black or dark like it
otherwise would. And this is also why you would add lemon juice
to avocado when it's just sitting out before adding it to a salad-you then inactivate these enzymes. The lower pH messes enough
with the enzymes so that they will not cause these brown
compounds, and thus the avocado stays green.

What's true for all chemical reactions, regardless of whether

they're helped by enzymes or not, is that a small increase in

temperature, not so much that the enzymes are denatured but a
small increase in temperature, will usually speed up the reaction.
And sometimes even a large increase in temperature will do this.
And you know this intuitively from baking bread. You know that
you put the dough to rise at a somewhat warmer temperature. Or
you know that if you want avocados or bananas to ripen, you'll
leave them outside of the fridge.

Collagen is another example where Nathan told you that if

you slow cook meat, so you keep the temperature not too high
but at a temperature around 50-60 degrees for a long time, then
this is enough to slowly break down the collagen over time. And
this would take a very, very long time if you were to just do it at
room temperature. But that small increase in temperature is
enough to make the reaction happen faster. So temperature
increases the reaction rates. Another way to think of this in terms
of our reaction diagram, is that an increase in temperature
somehow manages to make the reactant molecules turn into
products more easily. And so this increases the likelihood of a
reaction to happen. So if you think about this, if you wanted two
molecules to react with each other, you needed to increase the
likelihood that they would be in a position so that they could
react. And one way to do this would be to just make them move
around more. And then the likelihood of them bumping into each
other and causing a reaction would increase.

So how would we do this? We would increase the

temperature and then they would move around more. All of this
is described in what's called the Arrhenius equation. Arrhenius
basically described the effect the temperature has on the rate of a
reaction. And here is this equation. So the Arrhenius equation
says that k, which is the rate of the equation, equals k0 times e
the negative delta u over kt. So k is the rate of the reaction. And
k0 is the maximum rate that each molecule could have if it had
the maximum energy needed to get over that hump or get over
that activation barrier in the chemical reaction. Delta u is that
energy barrier. So the higher the barrier is, the more energy we
need, the higher delta u is. And kt, of course, we know from
before-- that's just the thermal energy. And so the higher the
thermal energy, the more the molecules move around, the more
energy there is for this reaction to happen.

So what this equation tells us is that if the thermal energy is

very large, then the exponent becomes very small, so it becomes

very close to 0. And e to 0, of course, is 1, so this means then
that the rate would be very similar to k0, which is the maximum
rate. So high temperature would mean a very high rate, very
close to the maximum rate. So really, if we have a very low
temperature, then the exponent would be very large. And this
then would give us a reaction rate that is very different, much
smaller, than the maximum reaction rate. And along the same
lines, if we had a very big delta u, we had a very big activation
energy, then the exponent would be large, and this would then
cause a reaction rate that was also much smaller than the
maximum reaction rate.

So this equation may look complicated, but it's really just

building on what you already know. You already know about

thermal energy. And it's telling us that there is some maximum
rate that a chemical reaction can have. And that the actual rate
then depends on an energy that you need to put into a reaction,
and how much thermal energy you have around. So in the case of
collagen, for example, and slowly heating the collagen at low
temperatures, what happens is that the collagen fibers, which is
this long string, it's a triple helix, will break down into gelatin.
And there are several steps to this, but one of them is hydrolysis
of the peptide bond. And so you can imagine as you slowly
increase the temperature, the likelihood of this peptide bond to
hydrolyze and break down into gelatin increases because the rate
of the reaction increases. And this is what happens when you
break down collagen, or in many other chemical reactions in
cooking.

Wylie Dufresne & Ted Russin Transglutaminase

So we are using an enzyme in everything we're going to be

doing today, and the enzyme is called transglutaminase. But we

refer to it affectionately as meat glue.

The culinarians at the table refer to it as meat glue. The

scientists at the table refer to it as transglutaminase. But maybe

you could talk a little bit about what transglutaminase is. It is an
enzyme, but what does that mean?

So we see enzymes in the kitchen all the time. We could

certainly wax poetically on enzymatic biochemistry, but we won't

do that. We see enzymes in the kitchen. If you cut a potato, if
you cut an apple, it'll brown. That's an enzymatic reaction. I'm
not sure, Wylie, if you've made cheese in your kitchen. You've
probably made cheese in your day.

Yeah, we've made cheese before. Certainly.

And you would add an enzyme, rennet to that. And that

would precipitate the kappa casein in the milk, and create that
physical, the curd. In our case, it's transglutaminase: Meat glue.
It's an enzyme that is capable of linking two different amino
acids, glutamine and lysine. And there is a reaction that this
enzyme catalyzes that allows these two to bond together and
create a covalent bridge. A covalent bond is a very strong type of
bond, and when chefs refer to this stuff as glue, it is a form of
adhesion. You're creating, you have two pieces that have now
become one, and there is a seam or a bond between those. In
this case it's a covalent bond, but it is ultimately glued together,
or adhered.

Enzymes, themselves, are basically proteins. Proteins are

composed of amino acids, long chains of amino acids. We see

proteins everywhere in the kitchen. Meats, Seafood, Legumes,
Soy beans, Poultry. You see them everywhere. Eggs. So proteins
are ubiquitous. More often than not they're structural. A muscle
tissue is a structural element in the kitchen. But you see them
everywhere. You see them in foaming. We make a meringue.
That's a denatured protein. Emulsifiers. They actually are able to
bring oil and water together, in different systems. So in this case,
specifically, we're talking about an enzyme, and what an enzyme
does is basically speed up a chemical reaction. It lowers the
amount of energy needed for the reaction to occur, and basically
creates an environment where that reaction is, energetically
favored. In this case, it is the bonding of glutamine and lysine.

Throughout the various demonstrations that we're going to

talk about today, and carry out, that reaction is happening. These
enzymes are sensitive to various environmental conditions.
Temperature. Time. pH. These different environmental conditions.
We're going to talk in detail about those conditions when we
come to the, particular demonstrations. But for now it's just
enough to say that pH, temperature, time, agitation, physical
proximity, these environmental conditions are central in the
enzyme's activity and the enzyme's ability to actively catalyze the
bonding of the glutamine and the lysine to create a bond, or
adherence, or glue.

Yeah, and we're going to take that reaction, and show some

pretty novel preparations. We're going to show some basic stuff,

sort of restructuring basic muscle foods. Taking a piece of fish,
bonding it to itself. Taking a piece of meat. Taking a thin cut,
making a thicker cut. Show some slightly more complicated
things. Noodles. Taking shrimp and completely restructuring it,
reforming it into an almost unrecognizable shape. And then we're
going to show how we can actually use this reaction, use this
enzyme, in systems that don't even have the requisite amino
acids present, by introducing those amino acids.

So you could create that texture without even having any

muscle tissue there. So yeah, in vegetables things like that.

That'll be great. Yeah, so let's go. Let's get to it. All right.

Transglutaminase

So in this first video, Wylie and Ted are going to show you

how they prepare the enzyme transglutaminase that they use to

make their remarkable dishes. And I just want to start-- before
they go and show you how they make slurries and things like this
with it --to remind you of a couple of basic facts about this
enzyme. So first, transglutaminase is an enzyme. It's an enzyme
that covalently cross-links amino acids to each other-- specific
amino acids. So remember, because the bond is covalent, it's
very, very strong. It can't be broken with heat or anything else
and that's really the magic that transglutaminase, or meat glue,
brings to the table when it's used while cooking.

So where does transglutaminase come from? So it turns out

that transglutaminase is a natural product. You have it within you.

I have it within me. Transglutaminase exists in plants. But it turns
out that the way that transglutaminase is purified or harvested
for use in the kitchen is with the help of a lowly soil bacterium
that a company named Ajinomoto figured out how to use. So
basically, these soil bacteria actually take the ingredients in their
environment and have been shown to produce quantities of
transglutaminase that can be used in the kitchen. It's a perfectly
natural process and product. And that's basically what is used.
Some of you might be concerned about issues with
transglutaminase safety and other things. And for that what we're
going to do is refer you to a cooking blog that Dave Arnold-remember our old friend with the eggs from the second week in
the course-- made, in which Dave basically goes through and tells
about the basic science of transglutaminase and also addresses
some of the concerns that some of you might have about its use
within food preparations. So the link for that is on the same page
as this video.

So now, before we turn it over to Wylie and Ted, they're

going to start their discussion by going through the different

types of transglutaminase that they use. Again, this product is
produced by a company, Ajinomoto, under the brand name of
Activa. And there are different types of Activa that are essentially
different mixtures of the enzyme with other ingredients that are
used in their recipes. There's Activa TI, there's Activa RM, and
there's Activa GS. And there are fairly simple differences between
the three of them. So Activa TI is essentially pure
transglutaminase. It's in a powdered form. It's the enzyme. And
in addition, it contains an additional component, which is really
just a filler, which is maltodextrin, which doesn't really have any
function at all other than as a filler. So the second type, Activa
RM, is also a mixture of transglutaminase and maltodextrin but,
in addition, it contains sodium caseinate. Now sodium caseinate is
actually a milk protein, so it contains amino acids within it. And
thus provides some support for the transglutaminase enzyme to
act upon when it's used in the context of the food.

So the third type is Activa GM. And Activa GM, it turns out,

is a mixture of transglutaminase, maltodextrin, and also gelatin.

So gelatin, of course, is also a protein and contains with it amino
acids for use in cross-linking the enzyme. The other interesting
feature about Activa GM is that it's held in a basic pH, because it
has a base that's added to the mixture. So the reason that this is
interesting is because it turns out that the enzyme
transglutaminase is inactivated under basic conditions. It doesn't
really work very well under those conditions. But, on the other
hand, meats-- the sorts of things that you're going to glue with
the enzyme --are slightly acidic. And the consequence is that if
you take Activa GM-- you make it as a slurry or whatever, you'll
see Ted and why we do this in a minute --and you then brush it
onto the meat, the pH changes because you've put it in contact
with an acid. And that activates the enzyme for its use.

When the slurry is sitting around the lab-- at least I've been
told --it doesn't lose its potency as it would if you were not to add
the base. So those are the three types, and we're now going to
turn it over to Wylie and Ted, who are going to show you first how
to make a slurry using these things, and how they prepare them
in Momofuku, in their kitchen. And then they will show us a
number of really remarkable dishes that they've been able to
concoct using transglutaminase as an enzyme. Enjoy!

Link to Dave Arnold's blog:

http://www.cookingissues.com/primers/transglutaminaseaka-meat-glue/

http://www.cookingissues.com/2011/05/20/the-trials-oftransglutaminase%E2%80%94the-misunderstood-magic-ofmeat-glue/

Wylie Dufresne Slurry

We're going to use three different kinds of meat glue

throughout the course of these demonstrations, Activa TI, which

is a pure form, Activa RM, which is sort of the workhorse, and GS,
which is generally used in slurry form. So you have to hydrate it
in some water, and then we're going to paint it on the things. So
it's got some interesting properties once you talk about them.
Yeah, certainly. Well, first and foremost, we have to get the
enzyme, in most cases, into solution, as you're talking about the
slurry. We certainly have RM, which is applied directly, and we'll
show an application of that. But as you can see sort of here, what
we're doing here is actually adding the enzyme without heat,
without anything, just sheer force. Yeah, in water. To get the
enzyme into solution. In fact, that water can't be too hot because
that begins to create activity. Yeah. In this case, ambient in
temperature. Protein, it's a protein. The enzyme is a protein. It's
a bit of a dispersion, the sugar that it's dispersed into it.

And, as you can see, it picks up air as it blends in the

blender, so we have to get the air out. We have to get the air out.
And this is a technique we use a lot to get the air out of any
various solutions. This is a vacuum chamber, essentially. So what
it does is just pulls. It's a sealed unit that pulls or drops the
pressure on the inside. Allowing, as you could see here, the
solution, the Activa solution or the transglutaminate solution,
actually bubble, literally boil because there's just very little
pressure there. You do this a few times to pull the air out of this
solution. And just whacks it on the downside. Yes. Ultimately,
once it breaks that vacuum, the environmental pressure of the
atmosphere will come back down onto it. So we're just pulling the
air out of it, as you can see here-- A couple of times. A few times.

Now, pulling the air out of it is extremely important from a

technique perspective. Yeah. Because we learned the hard way

that if you didn't pull the air out, all that air that was in the slurry
when we started, that you get all these little sort of micropockets between your bond or in your bond, and so the bond was
much weaker, and it would often just peel apart. So ultimately,
you want to have as little air in there, little pockets in there, to
create the optimum bonding surface. Your bonding surfaces to
surfaces. If you don't have any glue there, which is basically air,
then you won't create a bond. Right. The more air that's between
those two things, sort of the worse off we are. So that's how we
make a slurry.

Wylie Dufresne Shrimp Noodles

So in some of the earlier applications, we're gluing a piece of

meat to itself or gluing several pieces of meat to themselves.

What we began to wonder in the kitchen is, rather than gluing
something to itself, could we reshape it by actually pureeing it
completely and adding the enzyme, and it turns out that you can.
So in this case, we've taken shrimp, and we're pureeing it with a
bit of salt, a bit of cayenne, and not making a slurry this time.
We're not using GS. We're using Activa RM, which is better suited
to sprinkling. We're sprinkling that into the shrimp and making,
more or less, sort of an old-fashioned farce. We're not adding any
cream or egg whites or anything like that in the traditional sense
because we don't want to dilute the flavor of the end product, but
we're simply pureeing the shrimp. We're going to add a little bit
of shrimp oil to it made from the heads.

So in terms of what we're actually seeing here happen is we

have to get the enzyme into solution. When we pureed the

shrimp-- shrimp still, nonetheless, is basically mostly water. You
have the muscle fiber that we basically pureed, and you've added
the enzyme to this base with shear. You have gotten the enzyme
into solution, and now the enzyme is looking to create covalent
bonds. You don't have an unlimited time window to actually do
this. If you're not careful, I assume you can glue the shrimp to
itself in a pretty unappealing-

Well, what we're doing now is we're actually passing it

through a tamis, pulling some of the fibrous material of the

shrimp out, making a smooth, homogeneous, uniform farce that
is going to help the mouth feel, going to make it feel more like an
actual pasta, more like a noodle. But yes, you do have to work
quickly because if you were to leave this farce where it is now, in
the state that it's in, and come back half an hour, 45 minutes
later, it will have begun to set, and it would a problem. And keep
whatever shape it finds itself in. Yeah. But what we're going to do
now is we're going to take a little bit of shrimp oil that we make
from the heads and the carcasses and paddle that in to the meat
to give it a little bit of flavor and to also give the texture of the
noodle a little bit of elasticity. You know, the addition of fat into
any system like this, we see it in all kinds of different-- in making
a flan or [INAUDIBLE], or a creme brulee. The addition of fat
softens these things, changes the texture.

We're creating a three-dimensional matrix of protein bonded

to protein. With a little bit of fat in there, you can plasticize it,
make it a little softer. This is ultimately the goal, the aesthetic
goal, is to create a noodle, and noodles need to bend. Well, yeah,
and the oil helps to that end. And so we're going to put all that
farce with the oil into a bag, and then we're going to put that
into, basically, into an extruder, a very small extruder, and
through chemical shear, it's going to come out homogenized.
You're going to see, in a second, as we extrude it into the water
bath. But first we have to put it into this noodle maker. This is
just your traditional Japanese noodle maker. So we could,
theoretically, cut a hole in the bottom of the bag and just drop it
into a heating bath. But in this case, we're creating a particular
die, a particular size of noodle. Yeah. And we're actually
improving the texture by forcing it through that very small die.

Yeah. In a way, you're homogenizing it. You're forcing the oil

into smaller droplets, much like you homogenize milk from fat
milk. Sausage making. Sausage making, et cetera. And so now
we're going to extrude it into a bath at a very specific
temperature for good reasons. We had talked about in different
environmental conditions that govern enzymatic behavior. In this
case, temperature is one of those. When you have an enzyme,
and you glue it, and you put it in the fridge and let it set, it's a
slow reaction. In this case, at over 50 degrees Celsius, you drop
the noodle into that bath, and the enzyme works and works and
works very quickly, and you create a physical texture. You've
changed the architecture of that puree. And to finish the dish-it's a noodle made of shrimp-- we serve it with a little bit of
actual shrimp, some tomato sauce, some fried garlic, and some
basil. So it's familiar flavors in an unfamiliar form.

Wylie Dufresne Beef

All right, so in this case, we're gonna take a flap steak, a

Wagyu flap steak. The flap steak is from the, sort of the,
diaphragm. The back end of the diaphragm towards the hind leg
of the animal. And it's a very, very thin piece of meat that does
have some connective tissue surrounding it that needs to be
removed. So what we're going to do is, we're going to clean that
up, and then you're going to see, because it's a fairly thin cut of
meat, that we need to-- to be able to get a nice cook on it, a nice
sear on it, we've chosen to stack it. So again, Tommy's taken the
silver skin off, which is important, because there's no way we
could eat that silver skin, cooking the meat the way we would like
to. And he's brushing it with the slurry. And then he's going to
put-- much like the cut, he's going to put the piece of meat on
top of itself. Rather than stripping it and rolling it together, he's
going to stack it. And here he's just ensuring really good
coverage. He's going to paint the seams, to be safe, and he's
going to wrap it in plastic wrap.

Now, it is important to note, the silver skin, which is a

cartilaginous material, with cooking, silver skin would certainly

break down, but that would need time and temperature. And as
you can see, this cut of meat is relatively thin. If we were to cook
it long enough so that the collagen breaks down into gelatin and
gets creamy and juicy that way, by that time, the meat itself
would be over cooked. Because I believe the desired
presentation, or preparation, of this is not to have a braised
meat. No, this is not ideal for that type of cooking. We're looking
for, I'd say, medium rare to-- anywhere between rare and midrare, heading towards medium degree of doneness would be ideal
for this cut of meat. You can see, Tom's wrapped it up. Again,
contact points are important here. Pressure is not critical, but
he's wrapped it up, and we allowed it to sit, again, three to six
hours ideally. Overnight, if possible. And now we're going to
portion it.

Now, when you do look at the meat itself, it is almost

uniform. We had, again, time, low temperature, contact, allowed

for the development of an adhered seam. I think to the highly
trained eye, you could notice the seam, but to the untrained eye,
it's really just a nice chunk of meat, ready to be cooked the old
fashioned way. You know, again, we wouldn't be able to serve this
to the desired degree of doneness given the thickness or thinness
of the meat previously. Of course, the cartilaginous tissue has
been removed. And this allows us, again, we're trying to create a
sensory experience. We know where we want to go, but we have
to create the environment and the ingredients to allow for that.
So you look at that, and again, you can't really see where the top
ends and the bottom begins. And I think, again, that's why this
product is incredibly useful. We wouldn't be able to achieve this
cut of meat cooked this way, without meat glue, that's the
important thing to note here. This would be impossible without
this ingredient. And ultimately, the bond that this ingredient gives
to the system is heat-stable, allows for heating, allows for
forming, and ultimately for a uniform sensory experience.

Wylie Dufresne Cod

This first dish is cod with peas and coconut nori and a carrot

dashi. What we're going to do is a fairly basic application of meat

glue. In this case, we're going to take a side of cod and, as you
can see, fish, meat, most animals in general are not uniformly
shaped. And the flesh is thicker near the collar, thinner near the
tail. And traditionally in restaurants, that disparity in size is a
problem, and you end up with waste or you have to purpose
things, or not be able to use it. But in this case, what we're going
to be able to do is we're going to strip the cod. We're going to
brush it with our slurry so it's nice and evenly coated, and then
we're going to reshape it into a cylinder that makes it uniform
from end to end and eliminates all waste, allows us to control
portion size, cooking times, cooking temperatures, et cetera, et
cetera. So again, the meat, the flesh, the fish has all been nicely
and evenly stripped. And now we take that slurry and we brush it
on the fish.

What's unique about this slurry itself is that, while this is

transglutaminase, this is this particular grade that actually

incorporates some phosphate salts. And what phosphate salts
have the tendency do in this case is raise the pH. We discussed
enzymes and the various environmental conditions they govern
their behavior, and each enzyme has a particular range in which
it's particularly active where it can actually catalyze the reaction.
At high pH ranges, in this case eight, nine, transglutaminase is
not particularly active. So in that slurry that you see being
brushed on, that slurry itself is not particularly active. However,
as that slurry hits the surface of the meat, the buffering salt does
not have that high buffering capacity and the pH is dropped. In
that case, the enzyme begins to have its activity. Once it's hit the
meat, it's starting to glue and we have to get the meat in contact
with itself in order for those covalent bonds to actually be formed.
So you can see what we're doing now. Again, it's been brushed,
the reaction is beginning to take place. We have a limited window
in which we can make a nice clean bond.

So we take that fish that's been stripped, brushed, and now

we're going to roll it up. And what was once the misshapen piece
of fish is going to be a really nice, uniform piece of fish.
Misshapen is maybe not the kindest thing to say about God's
creation. But when you think about it from a culinary standpoint,
and when we're in the kitchen, we're applying heat, the more
uniform the object that we're heating, the better and more
predictable we can tell when it's finished cooking. And that's to
the benefit of the diner too. Let's be clear about that. We're not
just playing God here and making a turducken. We're actually
putting something in a very useful shape. There's zero waste
here, and this is to the benefit of not only the restaurant, but the
consumer as well, because we're going to be able to get
something very consistent, very uniform. And it pays respect to
the animal itself, because there's no waste. This is the entire side
of cod. Now what we're doing here is just piercing it a little bit to
get some of those air pockets out. Again, the effectiveness of this
bond is based on time and contact. And contact, physical contact.
So here they've been wrapped. It's been wrapped tightly. It's
also, while it may seem that no time has elapsed, once that cod is
wrapped, it is then put into refrigeration for a minimum of four
hours. Minimally three to six hours, ideally overnight. Overnight.

So as you can see, when we're unraveling this or portioning

this, no longer do we have disparate and separate pieces of cod.

In this case we actually have a uniform disc, a fillet. A puck of
cod, if you will. And each customer gets two of these. And you
can see, again, it's nicely marbled in a way very uniform. Very
easy to cook very consistently. We're just going to take these and
saute them the old fashioned way. Just a classically cooked piece
of fish in a pan, little bit of butter. And when you do look closer at
it, then you can certainly make out the different tranches or the
different pieces of the cod that were covalently bonded together,
or glued together. But, again, it's an interesting marbled effect. It
is, it is. It actually, I think, adds in a way to the sensory
experience of the diner. And you're eating something in a more
unique fashion. In this case, again, it's a piece of cod, two pieces
of cod sauteed, sits on top of a puree of peas and coconut. And
then the two pieces of fish, on top of that are some carrots
sauteed in butter. Then we make a pasta out of nori and we drape
it on top. And then that's a dashi broth made from carrot juice
instead of traditional water. So it's a cod surprise. It is,
underneath that cover. Lovely drape.

ATK Pesto

Pesto is a simple, versatile sauce that's easy to make in a

food processor. But many home cooks who try and make it are
frustrated when their bright green sauce quickly turns black, like
this pesto here. Why does basil darken this way? Well, when basil
is cut, oxygen mixes with chemical compounds, called
polyphenols, which are on the surface cells of the leaf. This
reaction causes the dark color and bruised appearance. The more
you chop the basil, the more polyphenols you are exposing to the
oxygen. And the darker it will get. And this is why pesto can turn
almost black.

However, basil is so prone to this enzymatic reaction that

even folding or rolling the leaves can break enough vascular

tissue and fibers on the surface of the leaves to cause
discoloration. And I've got two leaves here to show the point. This
leaf here was folded up, kind of rolled up a bit. And this one was
not. As you can see, there's lots of dark lines where that
oxidation is already taking place. Enzymes are biological agents
that increase the rate of chemical change and not just in basil.
Unlike many foods with strong flavors, garlic and onion have
almost no aroma in this state. No one cries when they're
shopping for an onion. But slice into that onion, and the aroma
can be overpowering. And that's when the tears can flow.

So what's happening? An enzymatic reaction similar to the

process that causes sliced basil to darken. Before slicing,

enzymes and amino acids are stored in separate sections of the
garlic and onion cells. When the cell walls are ruptured by a knife,
the enzymes and amino acids react with each other to create new
compounds. And these compounds are responsible for the
characteristic flavor of garlic and onion. In garlic, odorless sulfurcontaining amino acids come into contact with an enzyme called
allinase. The reaction of the two eventually produces a new
compound called allicin, which is responsible for garlic's familiar
scent and flavor. The more the garlic is broken down, the more
flavor you get.

So for example, minced garlic or garlic pressed through a

mincer like this, is going to have a lot more flavor than a piece of
garlic that I just slice very thin. In this garlic, I'm breaking a lot
of those cells. And I'm allowing a lot of that reaction to take
place. Here I'm doing much less cellular damage. So with an
onion, the process is the same. But the compounds created are
called thiosulfinates. Unlike garlic, onions also contain an enzyme
called LF synthase, which is responsible for producing the tearcausing compound, propanethial S-oxide. In the test kitchen,
we've tried more than a dozen purported home recipes for
keeping tears at bay, everything from freezing onions to lighting a
match while we're slicing them. But the best solution is to wear
contact lenses or don a pair of ski or swim goggles. What you
need is a physical barrier to protect your eye. If you don't wear
contact lenses, your best bet is a pair of goggles. Looks a little bit
funny. But it works. Also, using a sharp knife with a really good
edge will inflict less cellular damage and can actually limit
production of propanethial S-oxide. So you want to make sure
your knife is sharp.

So we understand how enzymatic reactions start. But what

about stopping them? One way to halt the enzymatic reactions is

with the application of heat. Heat deactivates enzymes, while at
the same time transforms these potent flavor and aroma
compounds into more pleasant forms. This is what happens when
you cook sliced garlic and onions. But you can also add another
ingredient to stop the reaction. In the test kitchen, we ran a
simple test with minced garlic for a basic vinaigrette with three
parts olive oil and one part lemon juice. In one batch, we added
one teaspoon of minced garlic immediately to the dressing. And
that's this batch here. In a second batch, we soaked the minced
garlic in lemon juice for 10 minutes. Then we made the dressing
with the garlic and lemon juice. Finally, in a third batch, we let
the grated garlic sit for 10 minutes, while we prepared the other
ingredients then, finally, mixed it in with the other ingredients.

So while these seem like small adjustments to the order of

operations, the flavor differences are huge. The citric acid in the
lemon juice speeds the conversion of that harsh-tasting allicin to
some mellower compounds, the same ones that are created when
garlic is heated. Soaking the garlic in lemon juice was a bit more
effective than putting the garlic directly in the dressing with all of
the other ingredients. But either approach is far better than
letting the minced garlic hang out for 10 minutes. In that sample,
the garlic flavor was overpowering. And it made for a pretty bad
dressing. So this is a really simple experiment. I encourage you
to try it at home. You'll really be able to taste the differences
yourself.

Now, what does all this have to do with pesto? Well, you can

use heat or acidity to keep sliced basil from changing color. Now,
you can find a lot of recipes on the internet that suggest throwing
a vitamin C tablet, otherwise known ascorbic acid, into the food
processor with the other ingredients. I have two bowls of pesto
here that I made two hours ago. The only difference is that this
one has 1 000 milligrams of vitamin C in it. As you can see, it's
bright green versus the one that doesn't have any. Now,
unfortunately, you can really taste the vitamin C. And it makes
the pesto unpleasantly tart. So this isn't really a great option. But
I have a third bowl of pesto here that I also made two hours ago.
Now, as you can see, it's pretty much the same color as the
vitamin C batch. Now, I can tell you the big difference is that it
tastes exactly like the darkened pesto. Well, that's because it's
made with the identical ingredients as the dark sample with just
one change. I blanched the basil leaves in simmering water for 20
seconds before processing them with the remaining ingredients.
And as I mentioned earlier, heat deactivates the enzymes that
react with oxygen to cause that dark color in the first place. And
the best part is it's completely effective. When we ran this test
and refrigerated the pesto for a week, it was still brilliant green.

The only trouble with this technique is that you need to

bring a pot of water to a boil. Then you need to shock and blanch
the basil in a bowl of ice water. So this method makes great
sense if you're turning a bumper crop of basil from your garden
into pesto that you plan to freeze for many months. But it's a lot
of work for a pesto you want to toss with pasta tonight. So I'm
going to show you a simpler way with the test kitchen's favorite
pesto recipe. Now, besides the color problem, a lot of pesto
recipes are out of whack in terms of flavor balance. And often,
the garlic is just much too harsh. So we solved this problem by
toasting it to mellow its flavor a bit. I'm going to add this to the
skillet here, pop it over medium heat. So I'm going to toast and
toss these around until they deepen in color a little bit, which will
take about seven minutes. And once again, we're using heat to
control the enzymatic reaction that's going to take place when we
put that garlic in the food processor.

OK. So this garlic has taken on a little bit of color. And it's

warmed through. So some of those enzymes have been

deactivated. What I'm going to do is just toss it on my board and
let it cool for a minute. Now, there's another ingredient in our
pesto that's going to benefit from some time in the skillet. And
that's the pine nuts. Now, with any nuts, heating brings essential
oils to the surface. It gives them a lot better flavor. Pine nuts
have a real tendency to scorch. So you want to use medium heat
here. And you don't want to walk away. Finally, you want to make
sure you shake the pan occasionally, so that you toast them all
over.

OK. So these are looking really good. You can smell the

aroma. And they have a nice brown color on them. I'm going to
transfer these directly to the food processor. Now that my garlic
has cooled a little bit, I'm going to peel it. And I'm going to give it
a rough chop, just so it's a little easier to break down in the food
processor. OK. That's great. Because this garlic is more mellow,
we're able to use a lot more in it in our pesto. So we have good
garlic flavor without it being harsh and bristling. Put this into the
food processor. OK. So with the garlic and pine nuts in the food
processor, it's time to add the basil. I've got a couple cups here of
nice leaves. And we're also going to add our secret ingredient,
which is a little bit of flat leaf parsley. Now, you won't really taste
the parsley, because we're not using a whole lot of it. But it will
have a really big impact on the color. Now, besides being pretty
brilliant green itself, parsley is a good source of the ascorbic acid,
which, as we saw with our vitamin C test, really helps stave off
oxidation.

Now, this trick isn't as effective as blanching, which will

really last for weeks. But it keeps the pesto green long enough to
toss it with pasta for dinner. So it's really the perfect solution
when you plan to make pesto and then use it the same day. So
I'm also adding seven tablespoons of extra virgin olive oil and a
half teaspoon of salt. Now, with everything in the food processor,
I'll put the lid on. And I'll process this until it's nice and smooth,
about a minute. I'm going to stop and scrape down the sides as
needed to make sure it's evenly processed. OK. So this looks
great. Nice and smooth. So I'll use my spatula to make sure I get
all of it and scrape it into this bowl.

Now, the final step is to stir in some grated cheese. And we

like Parmesan or Pecorino Romano in this recipe. I'm using a little

bit of Parmesan here. And this provides a lot of the flavor that
you get in pesto. OK. So you can see it's a really nice bright
green color. And having that parsley in there is going to keep it
that way for a decent amount of time. So the final step with any
pesto is you want to limit the amount of oxygen that actually
comes in contact with the pesto. And for this reason, you want to
press a piece of plastic wrap directly onto the surface of the
pesto. Another option is to pour a thin layer of olive oil over the
top, which will, again, prevent oxidation. So there you have it, a
nice, flavorful, bright green pesto that's going to stay that way.

PHILOSOPHICAL INTRODUCTION TO FERMENTATION

So far, when we've discussed proteins and cooking, we've

often talked about various ways of denaturing proteins, either by

adding heat, or by adding acid, or by adding a base. And this, as
we've talked about. it sort of messed up proteins, and this has led
to our idea of what it means to cook food. Now, if you did all of
these things to a living organism, to a living system, you would-because you're messing up the proteins-- completely mess up
that organism. And so, for example, if you were putting yourself
in 65 degrees, the proteins in your body would denature, and you
would die.

The same is true for when we cook an egg. We basically

cook the life that there was in that egg. So this may sound very
morbid, but sometimes when we're cooking we're actually using
organisms as a way to cook for us. And then we need to keep
these organisms alive. So this is what this entire week is about.
It's about fermentation reactions. And the whole point of this is to
use microbes, whether it be yeast or molds or bacteria, to
basically transform foods for us to create new chemicals that give
flavor and aroma and taste, and to preserve food, and so on. This
means that when we cook with microbes we have to be very
specific about the environmental conditions we have.

So when we bake bread, for example, we make sure that

we're not letting the dough rise at too low of a temperature, or

too high of a temperature. And this is because the dough will be
unhappy at too low or too high temperatures. But, if it's really
way too high, then the yeast is going to die, and it's not going to
create any bread for us at all. So when you watch the videos with
David Chang this week, you should keep this in mind about how
carefully he monitors the salt concentration, the heat, the amount
of oxygen there, and how all of this is very important in order to
keep the microbes alive so that they can do the cooking for us.

HAROLD MCGEE FERMENTATION

Hello. It's Harold McGee here talking with you this week

about fermentation, which takes us out of the realm of soft

matter physics temporarily, and into the realm of biology,
because food fermentations are the work of living microbes.
They're essentially invisibly small cooks that change foods very
much for the better, their physical properties included.

I find food fermentations kind of miraculous in an everyday

sort of way, and I make a point of experiencing that a couple of

times a week. I love yogurt, and I make it for myself from a
culture of bacteria that was given to me more than 10 years ago
by a friend from India. So I make it by scalding a quart of milk,
then pouring the milk into a tall jar, letting it cool to a warm body
temperature. And then, I add a couple of spoons of the previous
batch, which contain the yogurt bacteria. And I wrap the jar in
kitchen towels, and I just let it sit for a few hours. And in that
time, the bacteria multiply probably more than a hundredfold.
They eat up the lactose sugar in the milk, and they turn it into
lactic acid. And that change in pH changes the electrical charges
on the particles of milk protein floating around in the milk, and it
causes them to cluster together. And so when I unwrap the jar
after a few hours that initially-liquid milk has turned into a solid
gel. Of course, the flavor is very different. It's just magical.

Anyway, the list of foods that owe their deliciousness to

fermentation is, a long one, dry cured sausages, for example, like
salamis, pickles, breads, cultured, butters, the vinegar in a
vinaigrette, cheeses, chocolates, wine and beer and ciders and
the distilled beverages made from them. These are all the doing
of little creatures with long names like Saccharomyces cerevisiae
and Leuconostoc mesenteroides. They're all the bacteria and
fungi that do the real work of turning blandness into
deliciousness. Fermentation can be defined very generally as the
managed microbial transformation of raw plant and animal
materials into foods that resist spoilage. Above all, it's been a
method of preserving the bounty of a harvest or a hunt for
nourishment in leaner times. So peoples across the planet and
throughout history and prehistory have applied it to nearly
everything that's edible, fruits and vegetables and meats and
milks, of course, but even animal hides in the Sudan and fish
heads in the Arctic.

The most common food fermentations develop

spontaneously. That's how our ancestors discovered them in the

first place. And they're spontaneous because the microbes that
are responsible are all over the place, in the air and in the soil
and on surfaces of everything. And they thrive on the sugars in
nutrient-rich materials like plant tissues and animal secretions
like milk. And so as these first exploiters of the nourishment
multiply in the foods, they release a number of chemical weapons
that suppress their competition. And by doing that, they delay or
prevent the growth of microbes that would otherwise spoil foods
with disgusting or toxic byproducts. These various chemical
weapons include antimicrobial peptides, short amino acid chains,
but also lactic acid, acetic acid, which is what vinegar is made of,
and alcohols, all of which are harmless to us, in moderation,
anyway. And of course, some of them are addictively appealing.
So things like shredded cabbage and milk readily turn sour pretty,
much on their own. Crushed fruits get heady. And instead of the
putrid and inedible, we end up with sauerkraut, and clabbered
milk and wine.

Today, we easily preserve raw foods simply by chilling or

freezing them. That drop in temperature just slows all biological

and chemical activity, and so it helps keep them as they are. But
fermented foods are still popular, because they're actually better
than the original raw foods. They have more intensified and more
complex flavors. A piece of cheese is more delicious than a
spoonful of milk. A piece of chorizo is much tastier than steak
tartar, which is raw beef. The microbes themselves that are
involved in fermentations generate a lot of that complexity by
turning sugars into acids and alcohols and by breaking down
flavorless macromolecules, things like starch and proteins and
fats, into their components, sugars and amino acids and fatty
acids. And those building blocks have flavors of their own. They
also serve as precursors to other small molecules that we can
taste or smell. And then, the foods' own enzymes can do similar
flavor-generating work from within the food in the extended
lifetime that they get from the preservation effects of
fermentation. Eventually, all these changes go too far, and the
food becomes not so appealing and effectively spoiled. The thing
is that that point of that line between fermented and spoiled is
hard to define, and some fermented foods are actually popular
exactly because they flirt with that line between fermented and
spoiled. For example, there's a food called stinky tofu in China
which is made by taking vegetable trimmings and putting them in
water and just letting them rot over a few days. And then, you
soak the tofu in that same water so that they absorb some of
those rotten smells.

There's also an extreme version of herring made in Sweden

called surstrmming which is made by fermenting herring for

months in barrels in the summer sun so it's nice and warm and
the microbes can really get going. And then, they take those
fermented herring and put them in cans without sterilizing the
cans or the herring, so the fermentation continues inside. And it
involves bacteria that are also found at the bottom of the Great
Salt Lake. The way you can judge a good can of surstrmming is
by how much the can has swollen up to approximate the shape of
a football. Usually, swollen cans are a sign of danger and possibly
botulism, developing inside. In the case of surstrmming, it's an
indicator of quality.

And then there's natto, one of my favorites, which are whole

soybeans, fermented by bacillus subtilis, which makes them both

flavorful and really slimy. You've got to try them to appreciate
them.

Most food fermentations generally involve a community of

different microbes all growing at the same time or in close

succession to each other. But it's convenient to group them
loosely by dominant organisms and particular kinds of
fermentations. So by far the largest group is fermented by the
lactic acid bacteria, which of course secrete lactic acid. And they
produce an amazing array of our favorite foods, not just yogurt
and other dairy products, cheeses, and cultured creams, like
creme fraiche, but also pickled vegetables, everything from
sauerkraut and kimchi to ordinary pickled cucumbers, pickled
beets, that kind of thing. They also take care of dry cured meats,
salamis and chorizos and things like that. Fish sauces, also lactic
acid bacteria.

The second big group of food fermentations is produced by

yeasts, usually Saccharomyces cerevisiae, but also others. And

they produce alcohols and carbon dioxide from fruit juices and
other liquids that are rich in sugars. So of course, they give us
wine and beer and the distillates made from those things,
brandies and whiskeys and so on. They also produce breads.
There, it's the gas, the carbon dioxide, that matters, and the
alcohol, gets cooked out. And then, related to or kind of hanging
onto the alcoholic, fermentations are the acetic acid bacteria
which, if given the chance, will feed on the alcohol produced by
the yeasts. They produce acetic acid and turn wine and beer into
vinegars, wine vinegar, and malt vinegar. They also, however, are
involved in making chocolate. So cacao beans are the seeds of
the cacao plant. They come in a sweet fruit pulp, and the fruit
pulp is fermented to produce alcohol. The alcohol then feeds the
acetic acid bacteria to produce acetic acid, and it's the acetic acid
that actually seeps into the beans and changes their biochemistry
in such a way that they end up flavorful rather than bland and
astringent.

There's a third group of fermentations that's only become

well-known in the West very recently, and it's based on an Asian

method for fermenting starchy foods, mainly the seeds of grains
and legumes. So yeasts and lactic acid bacteria can't deal with
starch directly. And so sometime before the second century BC,
Chinese brewers domesticated a species of mold, a kind of
Aspergillus, that prepares starchy foods for the yeasts and the
lactic acid bacteria by converting the starch into fermentable
sugars. And at the same time that it does that, the mold
generates its own distinctive aromas. So it's with the help of this
Aspergillus, which is called koji in Japan, that sake and other
alcohols are made from rice in Asia. But it's also how soy and
tamari sauces and miso pastes are made. Those are very flavorful
seasonings often used in China and Japan and other Asian
countries.

Because Western brewers have always prepared grains very

differently for fermentation by yeasts, and that is by malting

them or partly germinating them so that they develop their own
starch-digesting enzymes, we in the West have only become
aware of the koji fermentation and its possibilities very recently.

Today's manufactured versions of fermented foods are often

just approximations, so many pickles that you can buy in

supermarkets are not really fermented. They're just vegetables
that have been drenched in vinegar and other acids. But people
have been continuing to make real fermented foods at home for
decades and decades. And in recent years, artisinal pickles and
vinegars have enjoyed a real renaissance. Professional chefs have
also caught the fermenting bug recently, and many restaurants
now proudly offer their own house-made pickles, and housecured meats. And some chefs are experimenting with those Asian
fermentations, applying them to non-traditional things like
cashew and pistachio nuts and chickpeas. These experiments with
what you might call fusion fermentation are probably just a taste
of things to come.

The James Beard Foundation is an American organization of

professional chefs which gives out awards of various kinds. In

2013, they gave the award for best reference book to Sandor
Katz's book, The Art of Fermentation, and it's really a superb
book. It's both a how-to guide for many of the familiar fermented
foods that we enjoy, but it also surveys dozens of unusual
fermentations that people have discovered all over the world. So
if you want to get a preview of what's likely to be showing up in
some of the more experimental restaurants, or if you want to
explore the world of fermentation yourself, then Sandor Katz's
book The Art of Fermentation is a great place to start.

INTRODUCTION TO MICROBES

Here are some pictures of all kinds of food. And my question

to you is what do all of these foods have in common? And the

answer is that they have all been produced with the help of bugs,
with the help of microbes, which is quite amazing. When we think
about cooking, we often think about heating something in pots
and pans, and stirring, and mixing. And, in fact, a lot of these
common foods are just produced with bugs. So coffee, which a lot
of us have every day, sometimes many times a day, chocolate,
wine, vinegar, yogurt, all of these, the very basics of them, their
very tastes are due to bugs.

So let's understand this. Here are some pictures of these

common bugs. So here is the yeast, for example, that we use

when baking bread or when brewing beer. Here is a mold, which
we use when making soy sauce. Here is lactic acid bacteria, which
we use when making yogurt. So this is what they look like on a
microscopic scale. So these are just some bugs. But lots of
different kinds of bugs have been used in food preparation. And
they've often been used for different reasons. And some of the
main ones are one, preservation of foods. Before refrigeration,
this was a major way to preserve foods. Another one is flavor
intensification. So, for example, soy sauce, which has very, very
strong flavors, all of this is due to microbes. And the third reason
is intoxication. So one of the earliest evidences of this is that
wine has been found in wine jars in what is currently Iran. And
this is wine that is 8 000 years old. And this is some of the
earliest evidence we have of how microbes have been used in
food to increase flavor, preservation, and intoxication.

Here's a map of a lot of different foods, from a lot of

different cultures. And all of them have been produced with

fermentation. So there is sauerkraut, there is preserved lemons,
there is natto in Japan. There's kimchee, there's soy sauce, there
is pickles. And all of these have different flavors. So you can think
of the very savory taste of soy sauce, and chocolate, which are
completely different flavor profiles. They're sort of covering the
entire flavor wheel. And all of this is due to microbes and the
compounds that they can produce. So how do microbes do this?
Microbes are really some of the niftiest creatures on Earth. And
they can live in a very wide environment.

So, for example, there are microbes living in the bottom of

oceans, near volcanic springs. And there are microbes in your

gut. And they are capable of turning just about anything into a
food source. And so what they do is that they turn big molecules,
carbohydrates, proteins, starches, into what's often small
molecules. And you already know this from Baking Week, where
yeast turns carbohydrates into carbon dioxide and ethanol. Both
of these are very, very small molecules. And similarly, a lot of
flavor compounds and aroma compounds are also small
molecules. And these are all due to the digestive enzymes that
microbes have. And so here are some examples of common flavor
and aroma compounds. And so this, for example, is the molecule
that gives you the taste of banana. And here is a molecule that
gives you see the taste of almonds. And here is another
compound, diacetyl, which is what gives you a buttery flavor.

So, for example, if you're drinking a every buttery wine, that

buttery taste is actually due to this compound. And this is the

same compound that occurs in buttermilk, for example. And
here's my favorite. This is what dirty, wet socks look like on a
chemical level. So here's a summary of how microbes do this on a
very general level. So most microbes are harmless for us. And
they're sort of everywhere. And so when we use them in cooking,
we often either use microbes that are already there or we add
microbes, such as when we were baking, we add yeast. And
these microbes then utilize the food as a food source. And as they
grow, they are kind of outgrowing all of the other microbes that
could possibly be hanging out in that food. And so they're out
competing them. And so this means that even a lot of the other
bacteria that are harmful, are also being out competed. And this
is what's giving that preservation of the food. And so the way the
microbes takeover is that as they're producing these foods
sources, they're producing compounds. And some of them are
kind of used in the chemical warfare against the other microbes.
And some of these taste very, very good.

Some of them are very flavorful. And other compounds are

produced as byproducts in this process. And these are very

flavorful and taste good. And so this is what's giving the flavor
intensification they we're getting from a lot of foods when they
have been fermented. And David Chang will show some amazing
ways that you can do this. So this, for example, is what's
happening when we're preserving vegetables this way. So olives,
and kimchi, and sauerkraut, they're all being preserved by
increasing the growth of bacteria that are living using the
starches and proteins as a food source. And as a result, they're
producing acid. And acid is often harmful for a lot of other
bacteria. And this kind of wipes them out and makes the food last
longer.

So another example of this is brewer's yeast. So what do

you do when you get a scrape on you knee and you want to
disinfect it? Well, you can use isopropanol, an alcohol, to kill all
the harmful bacteria around it. And brewer's yeast works the
same way. So alcohol it is toxic to most bacteria out there. And so
there are a couple specific strains that have learned to live in
alcohol. And they are able to then use the food source that other
bacteria are not using and kind of wipe those out. And still alcohol
is very toxic, even to brewer's yeast. And so people who have
brewed their own beer or wine know that depending on the yeast
strain, it can tolerate varying amounts of alcohol. But usually the
cutoff is around 20 percent. So this is why when you distill alcohol
and the alcohol percentage gets very, very high, you can open a
bottle of whiskey and you can have it sitting on your shelf for
years and take a little every now and then. But basically, the
whiskey does not go bad. And this is because of the alcohol
percentage. But a bottle of wine, which is anywhere between
10% and 15% alcohol, is going to keep for a couple of days. But
after that, it's going to spoil. And so you can't keep it on your
shelf for a very long time. And this is because of the lower alcohol
percentage. And the same thing happens with bacteria that use
lactose to produce lactic acid, which is what we utilize when we
make yogurt and other dairy products.

So this is a classic example of what microbes do. They take

a food source-- and in this case, it's lactose. And lactose is

actually very uncommon in nature. It's very common in the milk.
But in general, in nature, it's very common. So there is this
particular bacteria that know how to convert lactose to lactic acid
and use the lactose to grow on. And they then produce the lactic
acid. And this has a low pH, which wipes out all of the other
bacteria. And this is how this strain of bacteria lives. And we're
just utilizing this when we're making yogurt and sour cream, and
so on. Cheese is a great example of how very diverse these
flavors can become. So cheese can range all the way from very,
very mild flavors to almost kind of flowery flavors, to very stinky
and buttery flavors. And all of these are due to microbes. And, in
fact, as cheeses age, the community of microbes usually changes
to. And so when we make cheese-- and these days of course, we
don't leave things to chance.

We're actually inoculating milk with certain strains. And so

here is a list of some of the bacteria that we're using for making
Swiss cheese, for example, and other kinds of cheeses. And as
the cheese ages, it starts out with certain cultures. And then as
they grow and as the cheese changes, there is a change in the
communities. And different communities take over because the
food source is changing and they're able to kind of compete with
each other. And this produces the different flavors that emerge as
we age the cheese. Chocolate is yet another example, which has
a very, very different taste from cheese, where we take the raw
cocoa bean and we ferment it. And this gives us these very
intense cocoa flavors that we know as chocolate.

Yet another example is miso, which also has a very, very

different savory flavor. And miso is produced with two

fermentation reactions. And so, in this case, you're boiling rice
and you're then inoculating it. You're letting it sit for two or three
days. And then you take the rice and you add it to barrels with
soybeans and you let it ferment. And this is then what gets us the
miso flavor. So this is just rice and beans and fermentation. And
you get these very, very strong flavors. And David Chang is going
to show us how you can take this to a completely new level and
how you can really play with the different microbes you're using
to ferment foods. And he's going to show us how he has used this
to make completely novel foods that we haven't seen before. So
these are just some examples. But in this next segment, we're
going to look in detail at one of these reactions. And we're going
to take the example of wine. And we're going to look at how the
sugar in grape juice is turned into ethanol. And we're going to
figure out how theoretically this should turn out in terms of the
percentage of alcohol. And then we're going to compare our
calculations to an actual bottle of wine. So let's see what
happens.

DAVID CHANG INTRO TO FERMENTATION

So like he said before, a lot of our focus at the lab has been

developing the building blocks of our cuisine, trying to create an

identity for us as a restaurant group and the culinary world at
large. So our process is extremely similar to wine making and
beer making. We're taking seemingly mundane ingredients and,
through the microbial process, developing amino acids sugars and
stuff like that. So this version right here is made with all rye. And
the only ingredients in this product are salt, rye berries, started
with the rye koji and finished with cooked rye, and this
aspergillus right here. What's aspergillus, Ryan? It is a fungus
that basically eats the rice and converts the starches and the
sugars and the protein in the rice to amino acids, which as we
know is what gives us the flavor of the product. And for our
hozons, this is the liquid version of our product, this is the paste
version. And this one is made with only basmati and French green
lentil, salt, and aspergillus as well.

So aspergillus is a pretty amazing thing. When you drink

sake and you have those very floral notes, it comes from koji.
And what we do is we inoculate cooked rice and we sort of
introduce that into a cooked grain, or a cooked lentil in this case.
And we add a certain percentage of salt, and that's basically what
it is. It's not that difficult of a process, but getting the
measurements right and making sure that there's a cleanliness
and a safety factor is difficult, because we want to make sure that
we are working with stuff that could potentially go bad. And it
needs to be in a very controlled environment. So it's been a long
process working with Harvard, NYU, Cornell, and other smart
people that are much, much smarter than us that have given us
the green light to go ahead and do this

Aspergillus oryzae is a very, very amazing thing and I

thought we could study probably, whatever, a million different

types of microbes that we could probably collide with food and
create new flavors. But I feel that we could spend a lifetime on
aspergillus and I think that we could spend a lifetime just
studying rye and lentils. Yeah, the cool thing about our bonjees,
in the Northeast we have a great supply of hearty winter grains.
So we've kind of taken cues from the whiskey industry, and we
decided to try single grain varieties from the Northeast. So we've
tried farro, we've tried spelt, freekeh, hard winter wheat soft
winter wheat. And one of the coolest things that we've learned
here is how different each of those products taste from each
other. And that's the coolest thing to me too, is not only are we
not making it out of soy, we are really using local.

We are creating local flavors. We're in Brooklyn. I mean,

we're using a mold that evolved roughly a million years ago in

Asia, but for the most part, what are we making? It's something
that tastes vaguely Asian, tastes like soy sauce. But we're not
using anything that's Asian. All of these products are new York
based. Brooklyn based, for that matter. It sort of begs the
question, if we make lentils du Puy, lentils are famous in French
cuisine. If we make a dish based out of Gascony with foie lentils
and duck confit, but we season it with a lentil hozon, which is
fermented lentils, those flavors might have some Asian
characteristics, but the dish could look completely French. But
we're using Hudson Valley duck, lentils, everything from New
York. What are we making? So it's a question that we haven't
really figured out. And more importantly, because these
ingredients are so new to us, not the ingredients but the final
product, we haven't really figured out all the applications in terms
of making it. And that's what we're going to do today is show you
the process in terms of how we come about doing it. And some of
the new ways of fermenting, whether it be kimchi, which is a big
thing, but understanding the principle behind fermentation,
particularly lactobacillic fermentation.

DAVID CHANG HOZON AND BANJI

All right, so we're going to go through some of the steps of

making hoisin and banji. Again, the central ingredient at play

here is not the chickpea or grain or any legume. It's this rice right
here which has been inoculated with this stuff right here, which is
aspergillus oryzae-- as the Japanese call it koji. Again, it's a
fungus. It's a microbe. And we cook this rice at what
temperature? It's 212 steam, fully cooked. The important step is
to make sure that we're gelatinizing all of the starch in there. And
that's where the aspergillus really thrives, once all the starch and
whatever grain you start with has been gelatinized. And we want
to introduce and activate the aspergillus much like yeast. And
there's a certain temperature that you use it at. If it's too cold, it
won't work. If it's too hot, it will die. And the humidity's got to be
a bit right as well. Actually, perfect-- you'd need a perfect
environment for it to work. And that's what we have here. After
cooking it and introducing the koji, we now have this rice that's
been inoculated and ready to go and give its flavor to whatever
we choose.

Yeah, so this is basically like any other starter. This is all--

this is an analogy to winemaking. If we wanted to make wine, we

would introduce the yeast, or natural yeast. In this case, this is
our starter. So we're going to take this, which has its full of
enzymes, yeast. We're going to take that and add it to our base
flavor. In this case, we're going to do a-- this is farro. We're going
to do a chickpea banji. Basically, this farro's going to give it the
sugars and body and color. And the chickpeas are going to give it
a nice backbone, depth of flavor, and a little bit of sweetness. So
that's all we've done. We've cooked this. Cooked the chickpeas.
It could be-- again, like anything that's similar to a chick pea.
And we puree it. And we're going to incorporate the farro, and a
certain percentage of salt. Too high of salt-- the problem I have
with domestic misos is that they have such a high salt content
that it just tastes like nothing. And the really great misos that
I've tasted in Japan, it tastes like butter to me-- really rich butter,
or peanuts. Because the salt is almost-- obviously, it's present.
But not nearly present as in America.

Why would other producers of miso-- like massive

producers-- make miso with such a high salt content? Well, the
higher salt content means that they'll last a little bit longer in
your fridge. And it generally just keeps it a little more safe.
Especially, the larger producers are sending it out across different
countries and stuff. Us, we've specifically designed this recipe to
be a more lively and frutier hoisin than normally. And I found
that-- one of-- for me, the biggest gripe I have with high salt
content, like whether it's like 20% of its weight in salt-- is that
other people use in America-- is that the salt prevents the growth
of really delicious flavor. And it becomes really monotone. And the
less salt you use, the more sort of reaction you're going to get
with the microbial world and the more delicious flavors you're
going to get as a result. But I mean, it's harder to control. Which
is why larger corporations just don't want to mess with that.

So since it's just like three or four of us, this is stuff that we

can do. And we want to do it the slow way and the right way. And
we introduce it to the chickpea. And we add a small percentage of
salt, a much smaller percentage of the weight of chick pea and
salt. And then, what's next? So at this point, this is ground and
mixed with our starter, our koji. And then, it is put into our aging
room and pressed with about equal amounts weight. And then,
it's left for about a month anywhere to a year long. And one of
the reasons we age it-- we're still working out temperatures and
humidity. But it's got to be the right-- again-- environment for it
to continue to grow and to develop. Like if you store wine at 120
Celsius, it's going to die. All the beautiful things that are in that
bottle of wine are going to die. Or even if you freeze it, it's going
to die.

So the same range with our hoisin. We want to find the right

balance for its environment. And we're still in that process of

finding. It's different for a little bit of everything. So here we have
a final product of the chickpea. We've pureed it. And we've
actually pureed it again to sort of smooth out the texture from
the farro. And this is now what we call hoisin. So yeah-- like he
was saying earlier, this one has a very buttery, rich flavor to it,
but not too salty. And the cool thing about the-- what we were
talking about the salt before-- is this actually lends itself to a lot-a greater expanse of culinary applications than a traditional miso
would because of the lower salt content. A lot of the recipes we're
developing now are based around more on the pastry side. A lot
of our chefs-- Shawn Grieco has used this in an ice cream
application, working on doing croissant doughs with it and stuff
like that. And I find that it has a lot of notes of aged Parmesan.
And particularly, if we age it-- which we've done-- and try it out,
you can make-- we've done it. We've done pastas with aged
chickpea hoisin. And you're not-- it's completely dairy free. And I
make the joke that we're turning into a vegan hippie commune.
Because we can make a pasta now that has a lot of the notes of
Parmesan. It doesn't taste exactly like it. But if somebody's going
to eat it, they're going to be like, oh, it tastes like Parmesan. But
doesn't have any cheese in it at all. And then, it sort of begs the
question. Are you making something that's Italian? Are you
making something that's Asian? So you know, it-- not only on the
science level, trying to understand the sort of the semantics of
what it is is interesting too.

And so, this is our farro koji. And instead of using chickpeas,

we would just cook off just a raw batch of farro. And in the same
process, mix those two ingredients with a little bit of salt, little bit
of water. And then, press it for-- this one's about two months, a
little bit longer maybe. But it gives it just from those two simple
ingredients-- farro, salt, and aspergillus-- we get this great liquid
product with a beautiful body and dark color. This benji over
here-- the stuff that looks like soy sauce is not soy sauce. It
doesn't taste anything remotely close to soy sauce. But I don't
know. Again, it's delicious, but in a completely different way. It's
salty. It has beautiful caramel like notes, but it's not. And we
named it benji because it's based on a very loose interpretation of
the word bonjil. And I don't know how exactly, we just wind up
calling it benji. It just sounded better. Yeah, it just sounded
better. But you know, it just goes to show you that this farro, an
ancient Italian or Roman grain. And some that grows really well
here in New York. And we've taken something that is really
peasant food, and morphed it into a variety of products. All of
which have nothing to do with what it might traditionally be used
for. And that to us is exciting. We can take something that's
simple, and use it for things that have-- you know, use it for
simple applications now. So it doesn't all have to be complicated.

And another unique thing about this that we've learned is a

lot of the soy sauces that you purchase in your local grocery store
have been pasteurized and they have a higher salt content. Our
processes is unpasteurized. So it gives it-- it has-- and pretty
much across the board of most food items, the unpasteurized
version always has more character. And I think this one has a lot
fruitier and caramelly notes than just like a straight, rich soy
sauce would. Ryan spoke briefly about this being unpasteurized
product. And I think that's a very significant thing to talk about.
Eventually, you know, we're trying to figure out how to
pasteurized it to make it a little bit more shelf stable. But for the
time being, our product is unpasteurized. And if you've ever had
unpasteurized milk, you'll know what I'm talking about. If you've
ever had like the great, great dairy products in France-- like
unpasteurized butter, epoisses cheese that is grown in the
Normandy region of France. It's just a completely different thing.

So if you pasteurize something, you're cooking it at a certain

point to kill off certain microbes that might be harmful to you

down the road as you eat it. But in the meantime, you're also
killing off certain things that make the food more delicious as
well. So you just sort of get this very standardized flavor. And not
everything needs to be pasteurized. And this is something that
we're very excited about that we can sell that's very safe. A lot of
work has gone into making this unpasteurized thing safe, a lot of
testing. So this is something that I don't recommend making at
home at all. Definitely not making it at home. No, no, we have-yeah. Yeah. We've spent a lot of time doing that though. A lot of
time, a lot of money-- and we've had our help from a lot of great,
great people to make sure that what we're making is very safe.

WINE

So let's think more about how wine is produced, and why is

the alcohol content of wine usually somewhere between 10% and

15%. So if we think about this, we know that wine is produced
from grape juice. And grape juice has some percentage of sugar
in it. And we can find out how much that is. We can look at a
label of Welch's grape juice, and we can see that there's
approximately 20% to 30%. And so if we want to calculate how
much ethanol we would get from this, we can do this very simple
calculation. And so here is the balanced reaction of glucose
turning to ethanol and carbon dioxide. And if we balance the
reaction, we see that one mole of glucose is going to turn into
two moles of ethanol.

If we assume that grape juice has about 20% of glucose in

it, and we assume that we start out with as much grape juice as
we finally end up with in volume in wine, we can then figure out
what the final alcohol concentration would be according to this
formula. If we then assume that 20% of the volume is glucose,
then we end up with 150 grams of glucose, total. And if we
convert this to moles, that's 0.8 moles of glucose, which, since
there's a 1 to 2 ratio between the glucose and the ethanol, there
will be 1.6 moles of ethanol. And so if we convert this, this will
then correspond to 73 grams of ethanol. And if we know what the
density is of ethanol, we can find out that that's approximately
104 milliliters. And this in turn corresponds to 13.8% of ethanol
in this case.

So in the previous calculation, we're assuming that all of the

glucose in the grape juice is converted into ethanol. And so this is

why a typical red wine is not particularly sweet-- because it's all
been converted to ethanol. But what if you wanted a sweet wine,
or what, for that matter, if you wanted a wine with a higher
ethanol content? What would you do?

Well, one thing to do is you could simply go through-- have

the reaction happen-- and then you would just add some sugar at
the end. And you could either stop it there and have a sweet
wine, or you could have the fermentation continue, and the
microbes would make more ethanol, and you would have a higher
ethanol content. And there are different ways around the world
that people have tried playing with this. And one way is to simply
use sweeter grapes. And there are a number of different ways
that you can obtain sweeter grapes.

One of them is to just let them sit and dry on the vine, and

let the sugar content increase. Another way is to wait until it gets
cold outside, and the sugar content also increases. And that's
what's used for ice wines in Germany, for example. And yet
another way is to inoculate the grapes with a fungus, and this is
called noble rot wines. And there, the sugar content also
increases. And this is how you make Tokajis in Hungary or
Sauternes in France. If you now do this, you're increasing the
sugar content, and you're making a sweeter wine. Or, if the
fermentation continues to happen, you're making a wine with a
higher alcohol content.

So why can't you just increase the alcohol content

indefinitely? Well, the reason for that is that alcohol is basically a

poison to the yeast that are making the ethanol in the first place.
So after a certain percentage of alcohol, they start being very
unhappy, and eventually they die. And this happens somewhere
in the range of 17% to 20%, and it depends on what kind of
microbe you're using for this. That means that you cannot make a
wine that has an alcohol content that is higher than 20%,
naturally. And so if you wanted to do that you would actually have
to distill the wine, or have some other way of adding alcohol to it.

VINEGAR

So, as we just saw, alcohol can make foods resistant to

spoilage. But of course, in the world of microbes, there's always

going to be some bug who has learned to utilize a food source
that no one else can utilize. And it turns out there's also a bug
who can utilize ethanol, and turn that into food and energy to
live. So this happens if you just let wine sit around. If you
actually don't drink your wine, but you just let it sit on your shelf,
the way you would with whiskey, the wine will, over time, turn
into vinegar. So if you've ever opened a very old bottle of wine,
you may have had this experience, where you were very excited,
and then it just tastes really sour and disgusting and vinegary.

So two microbes that can do that are acetobacter and

gluconobactor bacteria. And so here's the reaction for the ethanol

turning into vinegar. So here's the ethanol, and it reacts with
oxygen. So this is under aerobic conditions, meaning there's
oxygen around. And this turns into carbon dioxide and acetic
acid, which is vinegar. Vinegar is actually a very powerful
microbial agent. It turns out that as little as 0.1% of vinegar in a
solution kills most microbes. And so if you have ever pickled-done a fast pickling recipe for cucumbers or other vegetables-you may have done this by not going through the actual
fermentation reaction, but you've just added brine, which is salt,
which is also antimicrobial. And you will have added some
vinegar, and this makes it keep longer. It's not true fermentation,
but it kills enough microbes so they can keep it for a long time in
the fridge.

So given what we learned from our calculation of turning

sugar into alcohol in wine, we can now use the same principle
and try to figure out how much vinegar we get from turning
ethanol into acetic acid. And so we can just use this equation that
we have here. And knowing that we started out with 1.6 moles.
And this is what we got earlier from our wine calculation. We
started with 1.6 moles of ethanol. And since the reaction is
balanced, we get 1.6 moles of vinegar, as well. And this is then in
a solution, which is a total of 750 milliliters. So we can divide
this, and we'll get a final concentration of 2.1 moles per liters. So
this would be our final concentration of vinegar in the solution.
And maybe from this we can now figure out what the pH of
vinegar should be.

So let's see if this works out. So the vinegar, of course,

sitting in solution, is going to-- it's not a strong acid, it's a weak
acid, which we learned about earlier-- so it's going to dissociate
into an acetate ion and into H+ ions. And we know, so we can
look up what the equilibrium constant for this is, and it turns out
is 1.8 times 10 to the negative 5. So if we then set up the
equation for the equilibrium constant, which is the hydrogen ions
times acetate ions over our initial reactant, which is the acetic
acid, this should equal the equilibrium constant. And we know
what our concentration of acetic acid is, and so we can solve for
our concentration of H+ ions from this, and this turns out to be
0.0061 moles per liters. And, of course, having our equation for
the pH, which is pH equals minus the logarithm of the H+
concentration, we then get at pH of 2.2, which is actually a very
good estimate for what a lot of wine vinegars are.

Now, if you don't do the fermentation all the way-- so, for

example, in balsamic vinegar there may still be some sweetness

left, and in other vinegars you may start out with different sugar
concentrations-- you will, of course, end up with a different pH.
So in some fruit vinegars, the pH is more like 4.55. But for the
case of wine vinegar if we assume that all of the sugar turns into
ethanol, and all of the ethanol then turns into acetic acid, this
would be the pH we get. And this is actually quite accurate. Here
now is a recipe for making your own vinegar from fruit, and, in
this case, it's a pineapple vinegar. So here we're starting out, not
with the wine and not with a normal sugar content, but we're
starting out with pineapple. And the recipe is a very simple. You
just take the pineapple, you add sugar. You then add some water.
And then you cover it with a cheesecloth, and you put it in a dark,
cool place from six weeks to six months, and every two weeks
you add some sugar.

So now, what we just learned about how this process

happens, every time you add more sugar, the sugar is turned into
ethanol, and the ethanol is then turned into acetic acid. And
gradually, over time, we're increasing the pH, which means that
fewer and fewer other microbes can live there, and the microbes
that are producing the acid can thrive and take over the solution.
So the important message, then, in all fermentations is that you
need to target the environmental conditions so they fit the
particular microbe you're trying to get more of. And so in this
case, we want a presence of oxygen. So that is why we're just
having this cheesecloth over. There is easy access to oxygen into
the solution. Whereas in other cases, as Dave Chang is going to
show us, sometimes you don't want any oxygen there. And that is
because you want to tweak the environment so that it is just
slightly enough favorable for some microbes, whereas the other
microbes are sort of taken over by the other ones.

MICROBE GROWTH

So Pia just showed you all of the remarkable things and

flavors in foods that microbes help us create. So let's now take a

moment and think about how microbes multiply. It takes a lot of
microbes to make many of the foods that she was telling you, so
they better grow very fast. So before we go and talk about
microbe growth, I wanted to start and talk about something that
might be a little more familiar to you. Which is, the multiplication
of people. How is it that people multiply? So you all know how
this happens. You start out with one person. And that person, of
course, divides and makes two people. The person who divided
then dies, so you're left with two people. Those two people
divide, making four people. The original two people die, the four
people divide, you then have eight people. And in the next
generation you have 16 people, and then 32 people. And there's
just proliferation of people.

So mathematicians call this process where one gives rise to

two, which gives rise to four, and so on, exponential growth. And
we can easily quantify this by writing down a formula for how
many people there are after N generations, according to the
model that I just gave you. The formula is this. The number of
people N is equal to 2 to the little n, where little n is the number
of generations. Now this tells you the number of people in terms
of the number of generations, and it reproduces the proliferation
that I discussed a moment ago. So if we want to convert, instead
of talking in terms of generations, we want to talk about time,
then what we can do is say that every generation takes some
amount of time.

So for humans, I don't know, you might say it takes 20

years, you might say it takes 30 years. So that means that n, the
number of generations, is the total time that's elapsed, divided by
30 years. And we can then write the formula as capital N is equal
to 2 to the t over tau. Where tau is the generation time, and in
this case it is 30 years. So why is this called exponential growth?

So the reason is is because mathematicians like to write this

formula, instead of in the simple form that you see in front of

you, we like to write that N of t, the number of people times t, is
e to the k times t. Where e is the exponential function and k is
what we call the exponential growth rate. k can be related to the
previous formulas that I gave you. It's simply the log of 2 based e
divided by tau, that is k. And this is simply a way to rewrite the
formula, and it gives the name exponential growth.

Now if you were to actually go and look at a plot of the

number of people that there were on the planet as a function of

time, as I show here, then what you would see is a function that
looks very much like the one that I just drew. The number of
people started out very small. And over time it rose. And now
there are lots and lots of people that are on the earth. And of
course, as you can see, if you look at this plot, the issue that it
raises is that eventually you might worry that all of the people
can't survive on the planet that they're in. Because they might
get crowded, or they might run out of food, or something else.
And indeed, one of the most important questions in the study of
sustainability of the earth is basically how this process will
proceed, namely, how many people can the earth support
anyway, given the food resources there are.

Now this is a topic that brings us a bit afar from the topic of

microbes and cooking, in a certain sense. And I'd like to just

recommend a book for you to read if any of you are interested in
this. There is a wonderful book, which actually is by the same
title, How Many People Can The Earth Support? that goes
through in great detail how this exponential growth formula that
I've shown you, combined with the resources that are available
on planet Earth, lead to a bound of the number of people that we
can have.

OK, so why am I telling you this in the context of a cooking

course? The reason, of course, is that the same issue occurs with
microbes in cooking. So in fact a microbe really does start out as
a single organism. For example, here's a picture of a bacteria.
And every generation, the bacteria divides. So one becomes two,
two becomes four, four becomes eight, and so on and so forth.
Until one has an exponential number of bacteria in a population.
After 12 generations, we have 4 096 bacteria. Whereas after 22
generations, we have more than 4 million bacteria.

So let's put in actual numbers to see how this works. So in

order to do that, we have to take an example of a bacterium. So

let's consider the bacterium salmonella, which is relevant for
cooking, because if there's too many salmonella in the food
you're eating, you will get sick. So it turns out that salmonella
has as a division time, under reasonable growth conditions, of
about 20 minutes. So this means that the number of salmonella
that there will be after time t, if you start out with one salmonella
on your piece of cheese that you are now eating, would be 2 to
the t over tau, where tau is 20 minutes. How many salmonella
will you have after 12 hours? So each hour corresponds to three
generations, because each generation is 20 minutes. So 12 hours
corresponds to 36 generations. So 2 to the 36, it turns out, is the
number 7 times 10 to the 10. So there are 7 with 10 zeroes after
it bacteria on your piece of cheese, if you start with one on it
right now. In 12 hours there'll be that many bacteria.

Will you be able to see them? Well every bacterium is

actually very small. It turns out that every salmonella bacteria

weighs about 10 to the minus 10 grams. It's 1 divided by 1 with
10 zeros after it grams. But if you wait 12 hours, until you have 7
times 10 to 10 of them, then that means that you will actually
have 7 grams of bacteria on your cheese. 7 grams is enough that
if we spread it out nicely, you'll be able to see it. And indeed,
that's what happens when food spoils. So if you take your piece
of cheese and you leave it on the counter without refrigeration for
some period of time, you will notice that on top of it, you will get
these wonderful films of bacteria or other microbes. And these
bacteria you can see, because the generation time of the bugs is
sufficiently short that if you let them sit for awhile, you'll end up
with a visible number of bacteria.

So there are many different types of bacteria that exist on

the earth. And there are many different types of bacteria and
other microbes that are relevant for food. In turns out that 20
minutes is about the fastest division time that there is. And here's
the table of the division times of several common bacteria and
other microbes. So another particularly relevant division time for
cooking is that of yeast. Of Saccharomyces cerevisiae. And that,
it turns out, has a division time of about two hours. So there will
be far fewer yeast cells in 12 hours than there would be
salmonella. Now if we continue this further, then we are going to
run into trouble. If we wait 24 hours, starting from our single
salmonella, we will end up with of order 10 to the 21 salmonella
bugs. If each of them has the mass 10 to the minus 10 grams,
that means we will have of order 10 to the 11 grams of bug. This
number is absolutely crazy. So one ton is about 10 to the 7
grams. So that means that this is about 10 000 tons.

Now there's no way, starting from a little piece of cheese,

starting with one salmonella, even if you wait 24 hours, can you
possibly produce 10 000 tons of bacteria. And that is because
mass is conserved. The bacteria have to eat. They are, of course,
feasting on the cheese. And once there get to be too many, then
they will run out of nutrients and they will stop dividing. So
indeed, if you were to make a plot of the life cycle of bacteria
growing on a piece of food, or really anywhere, there is a
characteristic shape to it. Initially, at early times, the bugs grow
exponentially. Their number increases according to the laws that
I've just described. But eventually this actually necessarily
flattens out, in what biologists call stationary phase. And this is
when essentially the number of bugs is essentially constant
because the bacteria are crowding each other and interacting with
each other.

MICROBE GROWTH CONDITIONS

So the growth of bacteria, as I've been describing, is really

very important for cooking. As Pia told, bacteria produce flavors

that can be very special. They help produce products and catalyze
chemical transformations that are very important, like the
production of ethanol and whatnot. And so the way that bacteria
grow is really critical in cooking protocols and many of the things
that you will see this week, for example, from David Chang. So
I've been talking about the time of bacterial growth, and that's
clearly a very important parameter. And I told you that it was 20
minutes. But, in fact, actually the time for the bacteria to divide,
or of any microbe to divide depends on the conditions that they're
in.

So the growth rate depends on the conditions, and the two

most important conditions when one thinks about cooking

situations are the temperature that the microbe finds itself in and
also the pH of the environment. So if we were to plot the growth
rate as a function of temperature, the growth rate tends to be
positive over some range of temperature. There's some minimum
temperature above which the bacteria will grow, the temperature
has to be higher than a certain number for them to be able to
divide. And the temperature has to be lower than another number
for the bacteria divided. Outside this temperature range, the
bacteria won't divide anymore it actually will tend to die. They will
tend to extinguish themselves. So this temperature range is really
very important. The lower temperature range for bacterial growth
is the reason that we put food in a refrigerator. It's because if we
make the temperature cold enough, then bacteria won't be able
to grow, and microbes won't proliferate on our food. Similarly,
when we pasteurize or sterilize food to get rid of microbes, we
have to make sure the temperature is above the upper
temperature. And so implicit in many of our recipes is this idea
that if you would like to get rid of microbe growth, you have to be
outside of these temperature windows. And if you would like to
facilitate microbe growth because you're trying to actually take
advantage of the chemical transformations that the microbes
would use, you have to be within these bounds.

So the same goes for pH. So it turns out there's a range of

pH's where microbes can grow. There's a lower value and there's
an upper value. And in the same way that we learned that we
could cook food by denaturing proteins, for example, by putting
them in a particular pH range, we also can manipulate the growth
of microbes in this way as well. So what are these numbers? Let's
just take, as examples, two of the microbes that tend to be
important in cooking. So let's take E. coli and Saccharomyces
cerevisiae. It turns out that E. coli grow in a temperature range,
which is roughly between 10 degrees Celsius and 40 degrees
Celsius. The condition for maximum growth is very close to the
upper temperature threshold. It's about 37 degrees Celsius,
which, coincidentally or not, turns out to be very close to the
temperature of our own bodies.

So the other microbe, Saccharomyces cerevisiae is a yeast,

which Pia has already talked to you about, and that tends to grow
between a couple of degrees Celsius and 40 degrees Celsius. So
in both cases, and, in fact, in the case of many microbes, if you'd
like to eliminate growth, you need to get about 40 or maybe, to
play it safe, 50 degrees Celsius. If you do that, then microbes
can't grow. And similarly if you get well enough below 10 degrees
Celsius, then they also can't grow.

DAVID CHANG KIMCHI

So one of the things that we had a total misunderstanding of

was making kimchi. And I think most people did until recently.
And we make a lot of kimchi at our restaurants. I just think it
tastes really good with noodles and, basically, everything. And I
thought that the proteins you add into making kimchi, which we'll
talk about in a second, were the reason for the fermentation
process. That's like saying-- I don't even know, it's just really
stupid.

So kimchi really is the foundation of Korean cuisine. Kimchi

is a general way of saying pickles. Not all kimchi is spicy. There

are thousands upon thousands of types of kimchi. We're making a
version of pechu kimchi which is a Napa cabbage kimchi. And
even within Korea, which is like the size of Florida peninsula,
depending on your region, you're going to have a different way of
making that kimchi. Some are going to have oysters. Some are
going to have to saeujeot, which is a salted krill shrimp. Some
are going to have fish sauce. Some are going to have mackerel in
it. It's a completely different way of making kimchi all over Korea.
And that's just one form.

The best way I can describe it is like barbecue-- everyone

does it a little bit different way. But you can kimchi just about
anything-- from blue crabs, to radishes, to any type of vegetable,
really. And again, not all kimchi needs to be spicy. More
importantly, there are many ways of making kimchi. And from
this point forward we're just going to say kimchi. And we're going
to make what is our version of pechu kimchi, a type of kimchi
that my mom does not appreciate at all, the way we make. And
probably most authentic Koreans-- I guess I'm an authentic
Korean, right-- wouldn't find it agreeable. But we sell a lot of
kimchi, and we needed to figure out a way to expedite the
fermentation process, which is actually lactobacillic fermentation.
So we made this, and then it turned out to be an accident in
terms of why it worked out, after the fact, and I'll explain as Ryan
goes through the process.

So we've previously seasoned Napa cabbage-- washed and

cleaned Napa cabbage-- with salt and sugar, let it sit overnight at
around room temp so that we're losing some of the liquid here.
How much liquid? So, about one head of cabbage. Yeah, I would
say it's about 40% loss of water. And as with most things in life,
we're full of water. So the less water in the lacto fermentation it
will speed up the process. So that's part of the reason why we've
salted and drained it. And one of the differences why we chopped
it up is, traditionally, you just quarter Napa cabbage, and you
make your kimchi paste or slurry, and you fold it into the leaves,
and you roll it up, and you weigh it down. And you eat it in, like,
three months at an ambient temperature. We don't have that
time, and more importantly, we don't have that space. We're in
New York City and we just have no space.

So how do you facilitate innovation in kimchi? How do you

facilitate that process to make it faster? How do you do it in a

week? And that's something that we did by accident and now we
know. All the steps we are doing are found in making kimchi.
One of the things that we don't do-- I mean, traditional steps that
people don't do-- is we add sugar to our kimchi, and we also chop
ours up finely, all to facilitate a faster lactobacillic fermentation.
And one of the things we discovered-- this is similar to
sauerkraut, and having made sauerkraut many, many times at
various other restaurants in my past-- was, putting it into a box
in a dark corner in a room temperature room isn't the magic that
makes it turn into sauerkraut. And neither is adding protein or
chili or whatever, or just the process of making kimchi.

The magic of making kimchi is the fact that the

microorganisms-- two organisms that create the lactobacillic

fermentation-- happen because they are already naturally
present, high, in Napa cabbage, and cabbage in general. And
when you add the cure which we did that extracted all this water
out, it creates an environment that is very conducive for these
two organisms to start converting sugars into lactic acid. And
that's how you get that fermentation process. Also since we cut it
up smaller, into chunks, it's going to obviously work faster. We've
added sugar to our cure, something that is not found in
traditional kimchi making, again to expedite that process because
adding sugar in a lactobacillic fermentation process really is like
adding steroids to it. So that being said, we'll go from the next
step. So the other two vegetables that we use are scallions and
shredded carrots. So those are basically just the three vegetables
that are in this product.

And then we have a kimchi sauce base that is made with

garlic, ginger, gochugaru, brine-- What's gochugaru? It is a

Korean chili. Do you know when it was introduced? I do not.
When was it, the 15th century? Koreans have only had it for 500
years. I can never remember exactly. The Portuguese introduced
it. So all kimchi before, say, 1600 was white and not spicy. And
we can thank the Europeans for the chili pepper. But one of the
things that we do here that's a little bit different is, we don't add
what is a very traditional way of making kimchi, is a rice powder
slurry, which also probably accelerates or acts as a sort of
enhancer of the fermentation process. We just don't do it because
I don't like the texture and we're already adding the sugar. So
this is pretty spicy and funky, a lot of garlic. Yep, yep, lots of
garlic, ginger, the brine shrimp also add more salinity to help the
lactobacillus grow and transform the cabbage. The brine shrimp
is, in Korean, called saeujeot. And we have some fish sauce too.
Yep, fish sauce. Yep. And we're going to sort of make this. This is
basically our starter. Yeah, I would never have thought of saying
that-- starter.

So it's important to break it up and bruise the cabbage

slightly. You want to throw some more in there? So at this point,

once we've seasoned it up, tasted it, we press it. Another
important factor to the lactobacillus growth is being in an
anaerobic environment. What's anaerobic? Without oxygen. This
is fresh kimchi. It's not fermented at all right now, and it's
delicious. I mean, it'll give you crazy funky breath, but it's very
delicious. And right now, another thing that we do to our kimchi
that is very different than most, and what my mom really
disapproves of, is it's very salty. We add more salt than most
people, but properly fermented kimchi-- you don't taste enough
salt because of the effervescence, which, I think, distracts from
the palate. And I think that it's always under seasoned.

So that's one reason why we add more salt than most. So at

this point, we'll put another press on top, probably with water or
something else that we find in the kitchen. And so as you see,
this one, it'll age for three months and then we'll end up with a
product like this. And you can already see from the color that this
one's a little darker and has gone through the fermentation
process. I like my kimchi after like a month. But believe it or not,
this has mellowed out a lot. It's not as spicy as it is fresh. And it's
just mellowed. And it sounds like a crazy word to use when
talking about kimchi, but it's not as fierce. Yeah, all the harsh
notes from the garlic, the chilies-- Have mellowed out. Yeah, the
funkiness from the cabbages, kind of all melded together. Much
more harmonious.

DAVID CHANG POMEGRANATE SEED KIMCHI

So one of the things that is beautiful about having other

people make kimchi that have no tie to making kimchi is that I

come up with ridiculous stuff. And the guys at the lab came up
with idea to make kimchi out of pomegranate seeds, which is like
I didn't really want to try it. But it's actually quite delicious. And
it's an interesting process because it shows you, again, what you
actually need to add to produce lactobacillic fermentation. It is
quite different than using cabbage. And I think it's interesting
because it shows once you understand the technique, you can
apply it to other things that are out there without making it a
bastardization of what kimchi is, because I think it's paying
respect to Korean culture, but using ingredients that we can get
here in America as well.

So without further-- So we started at a couple of

restaurants. We needed apple kimchi, so Felder and I, we tried to

think outside the box and tried to figure out what other products
we could use to lactoferment. And one of them we came up with
was pomegranate. And the unique thing about this product, it
doesn't naturally have any lactobacillus bacteria on it. So we
thought OK, we could take some whey from an unpasteurized
yogurt as a kick starter to see what would happen.

So Ryan, what's whey?

So this is the liquid runoff from the yogurt. And this

unpasteurized yogurt is cultured with lactobacteria. So naturally

this has got a good amount of lactobacteria still left in it. So we
use this as the starter instead of just naturally letting the napa
kimchi, which naturally has lactobacteria on it, we've introduced a
third party to get this going. So we'll add a little bit of that. It's
about 1% by weight. And similar to the kimchi and stuff, we
always have a mixture of salt and sugar, a nice fuel source for the
lactobacillus.

But again, if we didn't understand the principles of the

science, literally, of making kimchi, we could read books about it

and know, OK this is how you make kimchi. But if we actually did
not know the science and microbiology behind making kimchi,
something like this would never, ever, ever happen. So I wish I
had paid attention more in school when I was younger. There's
always enough time. I know. Always more time to learn. G.I. Joe
was right. Knowledge is half the battle.

So another problem solving thing that we came across was

the cabbage is a little softer, so it'll naturally compress to get that

anaerobic environment. The pomegranate seeds are little stiffer
and there's always pockets of air and stuff, so we decided to
Cryovac it.

What's Cryovacing?

It is reduced oxygen packaging. So it basically will take all

the oxygen out of here, and be in an anaerobic environment

similar to the pressed kimchi. So once this is put through our
Cryovac machine, after about 15 hours you end up with a bag
that looks like this. There's air in here now. What's in here? And
it's hot. Why is it hot? Well to start the fermentation, we need to
have it about body temperature. That's where the bacteria does
best at. And why is there air in there now? Because in the
vacuum process, that sucks out all the air.

Yep, yep. So what's in here now? So through the process of

the lactobacteria eating the available food source, the natural

sugars in the pomegranate, the salt and sugar that we added to
it, it's expelling gases, CO2. And that's how you would get this
inflated bag. So it's basically the enzymes eating the food source
and expelling gas. And we've made enough kimchi over the years
in bags, because I really like making kimchi in bags because I
think, again it expedites the kimchi making process. You have to
be careful, because it produces so much CO2 that the bag, or
sometimes your jar, will burst if you have not packed it carefully
with consideration that it's going to expand. So it's something to
be careful of. Yes we had a huckleberry accident last summer,
which was fun. That's pretty good. Tastes good. Really delicious.

I think what's important is not just fermenting because it's

cool and fermenting makes everything more delicious, because it

does. Fermentation was created, really, to store food. So this is a
great way of preserving pomegranates for the season and as it
ages, it's only going to get more delicious and more intense. And
that to me is always more interesting, because right now we're
trying to make things more frugal and all this stuff. But these are
techniques that we all need to know how to do. I think we're
adding value somehow. I think when most people think of
preserving, they go straight to pickling and stuff. I think this
version of lactofermenting these pomegranates, it stays a lot
truer to the initial product. So it's not so acidic, and it's still got
that fruity funk to it. And acidic in the sense that if you were
going to pickle pomegranates, or some type of fruit, you might
boil the hell out of it, get the pectin or add vinegar to change the
pH so it'll remain shelf stable. This is a completely natural way.

MICROBE DEATH

These facts are important to understand the protocols that

are put forth for food safety. Now, there are really two different
ways of actually eliminating microbes from food. The first is called
sterilization, which essentially means that you do something
which is sufficiently severe that you kill all of the microbes in your
food. And a second idea is that of pasteurization, which basically
means that you decrease the number of microbes substantially to
put them below some sort of safe threshold. So the definition of
what a safe threshold is really depends on the different type of
bacteria. And in the United States, the USDA has various
standards of what a cook needs to accomplish in order for food to
be declared to be safe.

So for the microbe Listeria, the standard says that you need

to decrease-- whatever the heating procedure, the pasteurization

procedure is that you use-- needs to decrease the number of
Listeria by a factor of a million. For the case of Salmonella, one
has to decrease the number of bacteria by a factor of 10 million,
whereas for E. Coli, the number has to be decreased by of order
100 000. So the way that the death of bugs works is very similar
to the way that the growth of bugs work. Namely, you would
imagine that every time, say every minute depending on where
you are, maybe half of the bacteria or microbes that you have will
die. So after a minute you have half as many as you had in the
first place, and after another minute you'll have half of that,
which is a quarter. Waiting another minute, you'll have a half of
that, which is an eighth, and then you have a sixteenth, and so
on and so forth. And so if the death time, as it were, were a
minute, then basically what you do is you divide the number of
bacteria you have by 2 to the n, where n is the number of oneminute intervals that you waited. And that will basically tell you
the way in which the bacteria are dying off to help you
understand whether or not you've met the USDA threshold.

So the rule of thumb that the USDA uses for this they call

the 6.5 log 10 rule. And what that means is that you're supposed
to wait long enough for the number of bugs to decrease by 10 to
the minus 6.5. Now, you'll notice the number 10 to the minus 6,
well, that's a factor of a million, that's Listeria, and they basically
recommend that you go a little bit below that just in case, and
that's the typical rule of thumb one has to obey when one is
doing pasteurization procedures. And presumably, that's to kill
the most-- if you don't know what kinds of bugs are in your food,
you want to kill the ones that are the hardest to kill to make sure
that you've got them all.

Now, if we set 10 to the minus 6.5 equals 2 to the minus n,

then it turns out that n, the number of generations you have to

wait to get this factor, is about 22. So the rule of thumb is that
you need to wait for about 22 generations of bacterial death in
order for it to be fully pasteurized. Now, the death rate, like the
growth rate, is temperature dependent. And so therefore, how
long this means you have to wait until the food is safe to eat
really depends on what the tau is, what the characteristic time for
the bacteria to die is, and that depends on the situation.

So just as example, let me show you a table from the

National Dairy Council of the pasteurization times that you need

to apply for milk. So if you do what is called vat pasteurization,
and heat your milk up to 63 degrees Celsius, you have to wait
about 30 minutes. On the other hand, if you do what is called
high-temperature short-time pasteurization, you can get away
with pasteurizing for only a second if you heat it up to about 89,
90 degrees Celsius. If you go up to 94 degrees Celsius, you only
have to go for a tenth of a second. And then there is this idea
called ultra-pasteurization, where you heat it up to 138 degrees
Celsius, and you wait for two seconds, long enough to make sure
that everything is really killed.

Now, one thing you should think when you look at this table

is that we've already told you what happens in this class if you
take milk and you heat it up. We've told you that proteins tend to
unfold at about 64 degrees or so, and so you can see that if you
were to actually heat something above 64 degrees, and heat it
long enough for the proteins to unfold, you would start to actually
cause phase transformations in the milk. So you can see that it's
important that when you undergo the pasteurization procedure
you don't let this happen. Similarly, I'll bet you if you go and look
at ultra-pasteurized milk in the grocery store, you will see it has a
slight brown color. The reason that it has a brown color is
because, of course, if you're heating at 138 degrees, you're
starting to initiate browning reactions, and you will see those
within the milk.

Finally, let me show you an equivalent set of data for meat,

for actually getting rid of microbes in meat. So here is a chart

that actually comes from Dave Arnold, and from his blog on
cooking issues. So what it shows is that it plots temperature on
the vertical-axis as a function of time on the horizontal-axis. And
so at every temperature it tells you how long you have to cook
something for it to become safe. The green regions on this plot
are places where you're totally good, if you put your food there
then you won't have a problem. And so you see, at the bottom of
the curve, that is below about 40 degrees Fahrenheit, or a little
above zero degrees Celsius, it's actually safe to store meat
without having microbes proliferate in them. And this,
presumably, many of you know, and that's the reason that we can
store meat safely by putting it in a freezer. There then is a large
red zone. This is a temperature range where there is not a time
that you can leave it to basically get rid of the microbes. This is
the region in which the microbes actually like to grow. And finally,
at very high temperatures, there's another green zone. If you
take your meat and store it above 75 degrees Celsius, then
basically the microbes won't grow there. And so you'll be OK. On
the other hand, what you also know is the meat will cook, and it
will even overcook, and so that you can't do, either.

So the question, then, is how can you actually take a piece

of meat which might have microbes in it and make it safe to eat?

And that is the role of the yellow zone. Within this yellow zone,
there exists some temperature where as long as you wait long
enough, the meat will be safe to eat. Notice on this plot there are
two different curves. There's a curve that corresponds to poultry,
and there's a curve that corresponds to beef. It turns out you
have to cook poultry slightly longer to make it safe than beef. And
so, for example for poultry, if you cook it at 60 degrees Celsius,
you have to wait about 30 minutes for it to be safe according to
this standard, whereas it takes beef more like five to seven
minutes to be safe.

Now, you might ask, why do you have to cook poultry longer

than beef? This, of course, is a question of which environment is

the growth rate larger, and although it's hard to say for sure what
microbes like and don't like, there's one observation that we can
make here, which I think is interesting to think about. Which is
that it turns out that the water content of beef is slightly less than
that of poultry. Poultry tends to be in the high 60's to 70% water,
whereas beef tends to be the low 60's% water. And one reason
you might think that that might be good for microbes, is that the
microbes, of course, want to be surrounded by water, and if
there's more space for them then they will be able to grow more
easily. There's more microbes you can fit in, actually, until the
meat is completely rancid.

28/11/2013 13:09:00

Bond Types

So in addition to the basic molecules of cooking, there's also

a few basic ways that the molecules of cooking can interact with
each other. Many of you have probably heard of these before, but
here's a recap.

So covalent bonds are very, very strong bonds, and these

are the bonds that hold molecules together. So in a fat molecule,

for example, the bond between the carbons, those are covalent
bonds. And the bonds between the carbon and the hydrogen,
those are covalent bonds. And since these bonds are strong, it
usually takes a lot of energy to break them. And so they usually
don't break until we apply a lot of heat, which we sometimes do
in cooking.

The second-strongest bond is an electrostatic bond, and this

is what keeps two ions together. So for example, the positive

sodium ion in salt and the negative chloride ion in salt, these are
held together by an electrostatic bond. And this is also a fairly
strong bond, relatively speaking.

If we're starting to think of bonds between molecules, there

are two kinds of bonds in general that we're interested in. And
one of them is also a strong bond if you're thinking on the
intermolecular level, and this is the hydrogen bond. So this is the
bond that is keeping the individual water molecules together in,
say, a glass of water. So a water molecule is one oxygen atom
and two hydrogen atoms. And when these interact with other
water molecules, the hydrogen ion is going to interact with the
oxygen ion, and this is a very strong bond that is also giving
water a lot of its very special properties. And this bond is going to
show up again and again in this course. So what's making the
hydrogen bond so strong is that there is actually a difference in
polarity between the oxygen and hydrogen. And with a difference
in polarity, I mean that the oxygen is going to be slightly negative
in charge, because it has a property that pulls electrons towards
it. Whereas the hydrogen is going to be slightly positively
charged, just slightly, and this is because the oxygen is pulling
away the hydrogens from it.

And so when there's not this strong difference in polarity

between two molecules, then we have what's called Van der

Waals bonds, and this is what occurs between molecules when
there is not a strong difference, say, between an oxygen and a
hydrogen. So for example, when the two carbon chains on a fat
molecule interact with other carbon chains, there is going to be
Van der Waals interactions that sort of hold them together. And
this is the weakest bond, but this is often broken when we boil
things or when we do other, more subtle things to food.

Chemical Reactions

Cooking involves many, many different chemical reactions.

When we cook food, bonds are broken and reformed within

molecules and also between different molecules. And when we
cook proteins, they denature and coagulate. And we're going to
learn more about that later on in the course. And then, of course,
there are browning reactions and Maillard reactions, and the
reactions between acids and bases that are common all the way
throughout cooking.

So let's remind ourselves a little bit about what chemical

reactions are about. So chemical reactions are a lot like recipes.

So here's a recipe for Molten Chocolate Cake, with all of the
different ingredients. And if we wanted to set this up as a
chemical reaction, then all of the ingredients would be our
reactants. And so here's a list of our reactants: butter, flour,
chocolate chips, and so on. And when we put all of these
together, we get Molten Chocolate Cake. And so, if this is a
chemical reaction, of course, we need to know how much we
have of each of these. And so, just like we do in a chemical
reaction, we would specify how much we have of each ingredient.
So we have 120 grams of chocolate chips. We have one stick of
butter, and so on.

Now, it's very important, of course, to keep track of how

much we have of everything. And so if we think of this as a

chemical reaction, then all of these ingredients at these particular
amounts will lead to eight small, Molten Chocolate Cakes. And if
we double the number of the reactants, we will end up with
double the amount of molten chocolate cakes. And so this is
called the stoichiometry of reactions. But of course, if we add all
of these ingredients together, they don't just magically turn into
Molten Chocolate Cake. We also need to add heat. And in the
case of the Molten Chocolate Cake, the heat is at 350 degrees
Fahrenheit, and this is what's causing the product, the Molten
Chocolate Cakes, to happen.

Of course, another common chemical reaction is the

dissociation of hydrogen ions from citric acid. And so here, again,

I'm showing you the reaction where the hydrogen ion dissociates
from the citric acid. And this is also a chemical reaction. I told
you earlier that citric acid is a weak acid, which means that it is
releasing hydrogen ions, but it's not releasing all of its hydrogen
ions.

And so when we think about chemical reactions, we want to

know: how complete is the reaction? How much product do we

actually get? Now in the case of Molten Chocolate Cake, we hope
that we would have a complete yield of our Molten Chocolate
Cakes, and we wouldn't be stuck with some extra eggs and flour
floating around. And so this happens when we cook. But in the
case of citric acid, the reaction is not all the way complete. And
as is often the case in reactions, there is an equilibrium between
the reactants and the products. So there's constantly some
releasing of hydrogen ions, and at the same time, there's
constantly some amount of hydrogen ions that are being taken up
by the citric acid again. And so these two reactions balance each
other out. But when the reaction is at equilibrium, there is a
certain amount of product present. And if we wanted to quantify
this product, we would, write this like this. And we call this the
equilibrium constant.

So we take the number of products, and we divide it by the

reactants. And if the number is large, that means that we have a

lot of product, and the yield was very large. So most chemical
reactions are reversible, which means that they can go either
way. They can go back and forth. But a lot of reactions in cooking
are not reversible. So when we make our molten chocolate cake,
we're stuck with our molten chocolate cake. And in the case of
the cake, that's not a bad thing. But the cake does not easily fall
apart and then go back to eggs and flour and chocolate chips.
And that is the case with a lot of chemical reactions. So if we
were to write the equilibrium constant for molten chocolate cake,
we would divide the amount of molten chocolate cake by the
concentration of all the ingredients. And we would get a very
large number.

So just like in cooking, a lot of the chemical reactions have

an activation barrier. And the activation barrier is some amount of

energy that you need to put, in order for the reaction to happen.
So in the case of molten chocolate cake, this is the whisking, and
the stirring, and putting things together into little ramekins so
that we can then make the Molten Chocolate Cake. And if you
think of chemical reactions, there's also an activation barrier.
There's usually some energy we need to put in for the reaction to
happen. And a reaction will happen more quickly if there is not so
much energy we need to put in. But if there's a lot of energy we
need to put into the reaction, then the activation barrier is high,
and the reaction does not happen as quickly. And so this is the
rate of a chemical reaction. And that is important for many
different kinds of cooking as well. And we're going to talk more
about that later on in the semester.

So let's talk about a real chemical reaction that a lot of us

are familiar with. And that is a reaction between baking soda and
some acid. And in this case, we're going to talk about a vinegar
as being the acid. So in this reaction, if we're going to put up our
reactants that go to our product, we have the baking soda
vinegar that goes to some product. And if we're going to add
chemical names to this, we say that sodium bicarbonate plus
acetic acid, which is what vinegar is composed of, goes to sodium
acetate plus water, plus a gas, carbon dioxide. So when we cook,
it is the carbon dioxide that contributes to the fluffiness that we
get in cakes when we add baking soda.

So here's the chemical reaction written out with its chemical

formula. NaHCO3 is the baking soda, plus the vinegar, which is

CH3COOH. And that goes to sodium acetate plus water plus
carbon dioxide. And so we have written the little symbols after to
indicate whether things are gases or solids. And we look at the
reaction, and we see that it is perfectly balanced like this. There's
the same number of carbons, and the same number of
hydrogens, and so on, on both sides of the reaction. So what this
equation tells us is that if we put in one mole of baking soda, and
if there is enough of all of the other reactants, then we're going
to end up with a one mole of water, one mole of sodium acetate,
and one mole of carbon dioxide.

And so if we look at a typical amount that you would put

into, say, cookies, and in the chocolate chip cookies that Michael
talked about earlier, we put in one teaspoon of baking soda,
which is about five grams of baking soda. And so if we then
calculate, using the molecular weight of baking soda, which is 84
grams per mole, we can calculate how many moles there are of
baking soda. And if we do this, it turns out that the number of
moles is 0.06 moles of baking soda. And this, then, by definition,
should give us the number of moles of carbon dioxide.

So 0.06 moles of carbon dioxide. So it is a known fact about

gases, and we're going to talk about this also later in the course,
that one mole of the gas has the volume of 22.4 liters. And so
using this comparison, we can calculate that 0.06 moles of carbon
dioxide is the same as 1.3 liters of carbon dioxide. And so this is
how much gas is produced in this reaction. And this we're going
to talk a lot more about later on in the semester, but this is a
teaser to remind you about chemical reactions and the kinds of
things are good to know about them for the purposes of this
course.

Other books and resources

The following books cover various aspects of the science

contained in the course:

The Science of Good Cooking, Americas Test Kitchen

The Science of Cooking, Peter Barham

The Science of Chocolate, Stephen T. Beckett

The Science of Ice Cream, C. Clarke

Cookwise, Shirley Corriher

Keys to Good Cooking, Harold McGee

The Curious Cook, Harold McGee

Modernist Cuisine, Nathan Myhrvold, Chris Young, and

Maxime Billet

Ratio, Michael Ruhlman

Several of the guest lecturers have written cookbooks, which

may be of interest:

A Day at El Bulli, Ferran Adri

Sous vide Cuisine, Joan Roca

Made in Spain, Jos Andrs

A Perfect Finish, Bill Yosses

CR20: 20 Years of Sant Pau, Carme Ruscalleda
Flour: Spectacular Recipes from Bostons Flour Bakery +
Caf, Joanne Chang

Momofuku, David Chang

Harold in the Schlesinger Library

So this course is being offered by Harvard. And that's

especially satisfying to me because I wrote the first edition of On

Food and Cooking here in Cambridge. And I had no idea at the
time that it would ever be used as a textbook in a college course
on cooking, because at the time, cooking had absolutely no
academic standing. There were no food studies programs. There
are lots of them these days. Food history was not of interest back
then. There's a lot of interest in these days. And of course, there
were no courses on the science of cooking.

So I arrived here in Cambridge, newly married, knowing no

one, and figuring out what to do about writing this book and
quickly realized that I had been very lucky to end up in
Cambridge, because there were so many resources. This is before
the internet, you have to understand, so I had to go to libraries to
learn anything. And this area is rich in libraries. I use the General
Library at Harvard, Widener, and discovered there that most of
the books that they had on cooking were located not in the main
library but in a place called the Schlesinger Library and ended up
where I'm standing right now.

This is the Schlesinger Library for the study of women in

history. And they had and still have a fantastic collection of

cookbooks. So we're in the Schlesinger Library right now. And I
wanted to show you a few of the things that really struck me
when I was writing back then and things that told me something
about the role of science in the history of cooking that I had
absolutely no clue about. As I say at the time, there was no
interest among scientists in what happens in food preparation.
And I had kind of figured, ignorantly, that had always been the
case. But a few days in the Schlesinger library, and it became
clear that in fact, I was wrong. Scientists have been influencing
what cooks do for centuries.

So here are a selection of books that demonstrated that to

me. The first one here from 1681 is a book describing the
invention and use of the pressure cooker, which is something that
you'll be learning about in this section on phases and phase
change. 1681 - I had no idea that the pressure cooker went back
that far. They weren't especially safe back then, so they weren't
used as much as they are these days. But it was right around the
time that Robert Boyle was developing the gas laws that someone
realized that information, that understanding, could be used to
cook things in a completely different way.

Here's a book from early in the 19th century by Friedrich

Accum called, Culinary Chemistry: Exhibiting the Scientific

Principles of Cookery - hundreds and hundreds of pages on the
subject. So people were interested, once upon a time in the
science of cooking and bothered to publish treatises on exactly
that.

The discovery that I made in the Schlesinger library that

amazed me and delighted me the most was when I found that in

the middle of the 19th century, an eminent German chemist
decided to take a look at how people were cooking and see
whether it made sense given his understanding of what was
important in human nutrition. His name was Justus Liebig. He's
still well-known in a number of fields. And he should be
remembered with a grain of salt in the history of culinary science,
because he decided on a misunderstanding of the way human
beings make use of proteins in meat that the most important part
of a piece of meat was the juices, nutritionally speaking. He
thought that the so-called fibrin, the fibers that make up the solid
bulk of the meat were not as important as what was in the juices.
And so he thought the most important thing in cooking meat was
to keep as much of the juice in the meat as possible. And
therefore, what you should do when you're cooking a piece of
meat is to cauterize it, essentially to seal the outside with very
high heat to prevent the juices from escaping as you then cook
the meat through.

So he published this idea in a book called Researches on the

Chemistry of Food in 1847. I thought that was very interesting.

But then I noticed, as I kept working my way through the books
on the shelves, that some cookbooks that year had read Liebig
and had paid attention to his theories. And because science had
such cultural prestige then as it still does, even though the
traditional way of cooking was exactly the reverse of what Liebig
was recommending, they adopted his system. And that was most
strikingly clear to me in editions of cookbooks that came out
before Liebig came out with his theory and then after. There were
a handful of very popular cookbooks that came out over and over
and over again over the course of several years.

And so here's a cookbook by Eliza Acton, Modern Cookery

and all its Branches, which in the pre-Liebig edition says to cook
meat gently to begin with and then brown it with high heat at the
very end. And then a few years after Liebig's book came out, in a
new edition she says actually on the title page that she has
applied Liebig's principles as much as possible and then
completely changed the recipe for cooking meat.

So here was one man, a chemist, who changed the way a

whole country ended up cooking its meat. And most appalling of

all, his theory, in modern language, is essentially, searing meat
seals in the juices. And you still see people say that in magazines,
on television. It's still a tremendous misunderstanding among
people who cook. And it all goes back to a chemist in the middle
of the 19th century.

So often, science can help cooks. Sometimes bad science

can mislead cooks. Escoffier wrote a book called Le Guide

Culinaire, The Culinary Guide, around the turn of the 20th
century. Escoffier is one of the fathers of traditional French
cooking. And this book was the Bible for traditional French
cooking. You would think that the French, having their own
tradition and a very strong one -- they're kind of the gold
standard for haute cuisine and gave us that name -- you would
think that they would have their own ways of doing things and
wouldn't be swayed by theories from German chemists. But in
fact, if you look at Escoffier, even he essentially says the same
thing that Liebig does in much more flowery and impressive
language. But the theory is exactly the same. And it's just as
wrong in Escoffier as it is in Eliza Acton.

And then just a word about Julia Child -- she was living in

Cambridge while I was writing this book. I never spoke with her. I
saw her occasionally shopping actually but never worked up the
courage to introduce myself because I was still a nobody. But I, of
course, admired her books. And one of the reasons I admired her
books was that they were so thorough. They were a way of
introducing French cooking to American cooks. But she did so in a
really rigorous way and a very clear way. So I loved her books
and then had the chance to meet her over the years, had a
couple of wonderful conversations with her.

Not that long ago, her memoirs were published. And it turns

out that she was a huge fan of The Science of Cooking. She had
books on the subject. She referred to them all the time. And she
decided when it came time to write Mastering the Art of French
Cooking, what she wanted to do was subject every recipes that
they were working on to what she called scientific proof. They had
to work out perfectly every time. And she had to be able to
explain why it worked this way and not that way. And so she, in
her own way, even though she didn't claim to be a scientist,
didn't make a big deal of using science to write her books,
nevertheless relied on the most important aspects of science,
which is curiosity, skepticism, experiment, and confirming what it
is that you think you know.

So this is a room in which I learned a lot.

Harold History I

So the first slide is to point out that the application of

science in the kitchen per se is not a new idea. It goes way back,
and the idea of using it to innovate in the kitchen, goes way back.

So this is an illustration from a French book from the 18th

century, and the translation is right up there. It talks about

nouvelle cuisine in 1759. And in order to develop nouvelle cuisine,
you need to be a chemist. Back then, what that meant was you
need to know your materials. You need to understand what
they're composed of. You need to come up with new permutations
and combinations, new compounds, in order to meet the
changing tastes of the times.

The next slide shows even before that point, seven or eight

decades before, that the kitchen and eating experience were

transformed by a scientific discovery. That is to say, the discovery
of the gas laws. The fact that the temperature of a liquid that's
boiling depends on the pressure surrounding it. So you can use
that information to invent what Papin invented. He called it a
digester. We call it a pressure cooker. And in the next slide, you'll
see an excerpt from John Evelyn's report. He was a member of
the Royal Society. The members of the Royal Society were
generally bachelors, and it seems as though they were looking
always for excuses to go out and eat at someone else's expense.
And Papin would demonstrate his digesters. He would put
different foods in them, and then the Fellows of the Royal Society
would get together and have a party. And if you just read through
this, you'll see that, for them, this was a completely new
experience. Bones that were made to have the consistency of
cheese. Fish that are bony that don't seem to have bones in them
once they're done. The very best jelly he's ever tasted. So this is
science applied to cooking hundreds of years ago, and it made a
tremendous difference. Next slide.

This man, Count Rumford of Rumford baking powder. He's

the guy who endowed the professorship. He's not as well known
in this country as he should be, because he picked the wrong side
in the Revolutionary War. So he endowed professorships, but he
never came back after the war. He did most of his work in
Europe. He invented, essentially, our modern oven, a metal box
that we heat in order to get a temperature. He's also the guy who
did the first experiments on what's since become, kind of modern
20th-21st century orthodoxy for cooking meat -- very low
temperatures give you the best results. He figured that out
hundreds of years ago by cooking legs of mutton in his potato
dryer and discovering, by accident, that cooking in a potato dryer,
which only operates at, well, way less than boiling, gives you
much more succulent meat. He's also, as far as I can tell, the first
guy who did any kind of controlled food science experiment. He
was convinced that this technique was much better than roasting
over a fire, but he had to demonstrate it. And so he demonstrated
it by throwing a party, putting a leg of mutton, roasted over the
fire at one end of the room, a leg of mutton roasted in his potato
dryer at the other end of the room. And at the end of the party,
he weighed what was left of the two roasts, and there was a lot
more left of the fire-roasted mutton. Next slide.

And this is to demonstrate that you can be a chemist and

you can screw up. So this guy, Justus Liebig, very important
chemist in the history of the development of chemistry, took an
interest, unfortunately, in cooking. And he doesn't seem to have
done a lot of experiments, unlike Rumford. And he came out with
a theory in the middle of the 19th century that searing meat
would seal in its juices by cauterizing the outside, preventing the
juices from coming out. And there was clearly a hunger at that
time for some kind of rational approach to cooking. So in the next
slide, you'll see that a book that came out in multiple editions -and an edition came out after Rumford published his researches
-- now says in the subtitle that the principles of Baron Liebig have
been applied to cooking meat in this book, and therefore it's up to
date and it's scientific. And there's a quotation from another
holder actually of the Rumford chair. I forget his first name, but
Dr. Gregory. "It is the want of a scientific basis which has given
rise to absurd methods of preparing food."

The problem is, if you do the experiment -- and anyone

who's ever cooked a steak has done the experiment -- you always
see with your own eyes that there's no such thing as sealing the
juices in a piece of meat. But that's still something that you'll
hear said casually on TV shows, said, in magazine pieces. I've
been trying for decades to get it killed, but I haven't been able to
kill it. Next slide.

So there was a lot of interest in science applied to the

kitchen in the 19th century. What happened in the 20th century?

Because by the time I came on the scene, not much had been
written about it, and that's why I wrote a book. And I think it has
in part to do with a couple of developments. One of them is,
oddly, the development of home economics. That is to say, the
institutionalization of the scientific study of cooking, because it
took a very particular direction. Ellen Richards was the first
woman graduate of MIT. She helped found Woods Hole. She was
a remarkable scientist and pioneer in all kinds of ways, and she
also helped start the home economics profession in the United
States. But you'll see in the next slide that in order to make it a
respectable profession for a woman, you had to kind of situate it
correctly. And clearly, anything that appealed to pleasure rather
than to things like hygiene, safety, economy, and things like that
didn't count for as much. And so flavor in the writings of these
people who founded the discipline was relegated, essentially, to
the status of a contaminant. If you like something, it's because
they're bacteria that you're used to, and it has nothing to do with
the goodness of the food. So the recipes that you find coming out
of this movement are things like a mayonnaise where you replace
the olive oil with mineral oil, because mineral oil is not going to
spoil on you. Next slide.

There was also the food security issue in the United States.

Back then, it wasn't worries about terrorism and global warming

and things like that. It was simply worries about adulteration. A
lot of foods in the United States were adulterated, and so the
Pure Food and Drug Act was passed in 1906. That mandated
analysis of foods to prove that they were pure. And that meant
you had to have analytical chemists who would do that kind of
work, and that gave rise to the food science profession. Again,
nothing to do with pleasure, nothing to do with the process of
making foods. It's more to do with safety and things like that.

By the way, these are pictures of the poison squad, as they

were known. These were the people who would eat things to see
whether they made you sick or not.

Harold History II

Now I want to just give you a very quick overview. And this

is, I apologize it's such a caricature of a couple hundred, 300

years of culinary history, which is very rich. But just to give you a
sense of what the last 20 or 30 years have meant, why we're
here tonight. A very quick look at the professional kitchen preFerran. So next slide.

1750: a Frenchman writing about what it is that a cook

should be doing in the kitchen as a chemist. And the job

essentially is to harmonize, to get the essences out of foods, and
then to harmonize them, so that no particular element dominates
the others. Everything is there in a kind of balance. And I think
that basically holds true even today. That idea of balance and
harmony and so on is sort of at the root of what classic French
cooking is all about. Next slide.

Careme and Escoffier are two kind of landmark figures in the

development of French cooking. And basically, what they did was

start with that basic idea, and then elaborate on it. And by the
end of many, many elaborations, what you ended up with were
guidebooks, "guide culinaire", very, very thick, full of what
amount to themes and variations. Relatively few themes, lots and
lots of variations. And many of the themes have to do with meat
extracts. That's really at the base. Even most vegetable
preparations were finished with the sauce that came from meat.
So it's a very highly developed and wonderful cuisine, but it
occupies a fairly narrow part of the spectrum. Next slide.

The French themselves began to feel a little restless about

this in the late '60s, early '70s. And so, a new nouvelle cuisine
developed. And these are the Ten Commandments, that were
kind of formulated not by the chefs themselves, who tended to be
kind of mavericks, not about to make commandments for other
people. These were put together by journalists, who were trying
to understand the movement in general. And you'll see various
things that have to do, in fact, with eliminating brown and white
sauces, because they were so overused.

But two important things: seek out what new techniques can

bring you, and you shall be inventive. At that time, new

techniques, new technologies included things like electrical
blenders, which give you really, really fine purees, finer than what
you could make before, easily. And things like that, things that
would not be that surprising to us today. Next slide.

So we finally come to Ferran. And here he is. This is a

meeting in Cannes. And he's written about this in detail, and in

really fascinating ways. The fact that he went to this meeting of
French chefs, and heard the man who, standing at the far left in
this photograph, Jacques Maximin, say "to be creative means not
to copy." And that, for whatever reasons, resonated with Ferran
in a way that nothing else had, and that kind of changed his life,
and that changed the course of culinary history. And that's why
we're here tonight. Next slide.

Just to give you an idea of what creativity meant in Ferran's

hands as opposed to, say, the hands of the chefs of the nouvelle
cuisine. Michel Bras is a kind of second generation nouvelle
cuisine chef. Works in the Auvergne, greatly respected, all kinds
of things you could say about him. And by the way, the molten
chocolate cake that is going to be made in the course is his idea.
So that's why it's there. Next slide.

He is in a part of France, the southeast, which is very rich in

native plants that are edible, and that had not been used in
classic French cooking. And so, he thought that one of the things
that he could do would be to use the local things in season to
make dishes that were very special to his place. And so, he
invented something that he called the gargouilloun, in the next
slide, which is a miscellany of herbs, vegetables, sprouts, all
kinds of things that he would gather, or his people would gather,
in the course of the morning, and then prepare over the course of
the day. And each one was prepared separately, because a
different leaf is going to require a different kind of preparation.
You want to do each one perfectly. So this dish, which was
classical in a way but revolutionary in a way, quickly became an
icon. And people used it as a kind of reference point for the new
way of looking at cooking. So next slide.

This is what Ferran did with the same idea. He tasted and

experienced the gargouilloun. And as he's written, he thought

about it for a few years. What can I do with that basic idea, but
really be creative with it? And what he did with it is this, which is,
again, a mixture of, in this case, fruits as well as vegetables, and
an herb. But if you look at it, none of the components of the dish
look like what they came from. So Michel Bras takes the bounty
of nature, celebrates the bounty of nature, presents it to you as
the bounty of nature in a beautiful way. Ferran starts with the
bounty of nature, and then moves on to the bounty of the
imagination. What can we as human beings do with these
wonderful, natural materials to make them even more
interesting? Or if not more interesting, because it's not really a
comparison in that sense, what can we do with these things that
has not been done before, and that can you give us something
more from the experience of cooking and eating than we've
gotten in the past? So it's a commitment to a different level of
creativity, taking it as far as possible, opening the door as wide as
possible. Making food and cooking much more interesting, and
making the science of food and cooking much more interesting at
the same moment. Next slide.

So Ferran has what's essentially a research and development

laboratory, that worked on creativity, in particular, without other

distractions. And its resulted in just an amazing body of work,
body of accomplishment. Next slide, please.

Now a few examples of the kinds of things that this kind of

openness of mind has made possible for other chefs. And a

number of these people are, in fact, people who will be coming to
teach in the course, and to give public lectures. And so you'll be
seeing them if you come back. Jose Andres is right here. And I
put this up because this is one of the most beautiful dishes I've
ever seen. It's about that big, and it's olive oil encapsulated in a
material that's like sugar, but not like sugar. So it's actually more
versatile. You can do things with it that you can't do with sugar.
One of the things you can do with it is blow it the way you can
blow sugar. And so it's a drop of olive oil inside this very fragile
vessel, with a piece of the sea salt on top, a little bit of vinegar
powder underneath. So it's sort of the essence of vinaigrette
without the salad. You just pop it in your mouth, it's there, and
it's gone. And it's gorgeous. Next slide.

Wylie Dufresne is coming to use meat glue,

transglutaminase, to make things like noodles that are pure

shrimp. No starch, no filler, no binder. It takes care of itself. And
the best chicken nuggets you've ever had. Next slide. Joan Roca
is coming, and he specializes, among other things, in distillation,
which is a way of extracting aromas, and separating them from
the materials that they occur in. And then you can recombine
them in all kinds of ways. This is a dish that made a huge
impression on me. You can't really quite see, but it's an oyster
embedded in a jelly. And you bite into it, and you taste the oyster
right away. And then slowly, over the course of 15 or 20 seconds,
you feel as though you're walking through the forest. And it's
because he's taken a handful of forest soil, distilled it into just its
aroma, and then infused that into the jelly. Next slide.

So the last 20 years have been really amazing. And this

catalog, Raisonne, that the Tate Modern Museum put out of

Ferran's dishes is one testimony to that. It's also quite a
testimony that the creator's portrait on the book was done by the
creator of The Simpsons, which I think attests to a certain level
of, how shall we say, cultural significance. It's really a remarkable
20 years. And so, that's kind of why we're here. And now time to
listen to the real reason we're all here, which is to hear Ferran
and Jose to talk about their work. So thanks.

Moles

When most of us cook, what we do is take measuring

devices, be it measuring spoons, measuring cups, and we

measure various amounts of ingredients and mix them all
together, follow the recipe, and out comes what we like to eat. So
I'd like to show you now my favorite recipe. So my favorite
recipe, it turns out is the Nestle Tollhouse chocolate chip cookie
recipe, which is right here. And you can just look at this recipe
and imagine how you would make it.

So in this recipe, what you're supposed to do is take some

flour. So, the recipe calls for 2 and 1/4 cups of flour. You're
supposed to put in a teaspoon of baking soda. You're supposed to
put in some butter. You're supposed to put in brown sugar. You're
supposed to put in white sugar, a couple of more ingredients. You
mix it all together in the right way, and out comes the chocolate
chip cookie. So this is the standard way that we describe recipes,
and we describe cooking. But the point of this class is to try to
ask how it is that recipes like this work. That is, why is it that if
you follow the set of protocols that are given in this recipe that
you end up with Nestle Tollhouse chocolate chip cookies? What is
it about the ingredients that are giving rise to the properties of
the recipe? Why is it that when you cook the recipe for longer, the
cookies get browner? Why is it that if you don't put in baking
soda, they don' come out quite right?, Why should you use brown
sugar as opposed to just purely white sugar? Why does the recipe
call for a mixture of these two? These are the sorts of questions
that we would like to answer. And we'd like to try to understand
them in scientific terms.

Now, hopefully you all come to this discussion convinced

that actually the essence of a scientific discussion of a recipe like

this one are the molecules that make up it. So flour is composed
of starch granules, which themselves have molecules. They have
starches in them. We discussed to you that starches tend to be
chains of sugars. Butter consist of fats and also some water and
other things. Baking soda is itself an interesting ingredient. At the
essence of all of this are the molecules that make them up. And
so what I'd like to do right now is ask what I think is a very
simple question that might give you a slightly different
perspective on this recipe, which is how many molecules are
there? So can we take this recipe and rewrite it in such a way
that is instead of listing out the ingredients like they usually do,
what I want to do is list out how many molecules of each
substance the recipe is calling for.

As you'll see when we go through this, it's a little bit dicey in

places. But hopefully in going through this, we'll give you a spirit
about how to start to think molecularly. So how do you figure out
how many molecules there are? Well, in general, I'd give you two
pieces of advice. So first of all, you need to decide what the size
of molecule is. There are two ways of measuring size from the
point of view of this discussion. You can either know the volume
of the molecule, or you could know the weight of a molecule. The
volume, of course, is determined by its size. And the weight, well,
that's just what you would weigh it on a scale if you only could.
And then what you do is you take the stuff that you have. So for
example, in this picture, if we imagine that the blue square is my
hunk of food and the green square is my molecule, if I simply
compute the ratio of the volume, of the blue square to the green
square, that would tell me the number of green squares that are
needed to make up the blue square. Alternatively, what I could do
is measure the mass of the blue square. And I could measure the
mass of the green square, the little molecule, and then I could
divide the mass of the blue square by the mass of the green
square. And that would also give me the number of molecules.
And those are really the two ways of measuring the number of
molecules.

And so what I want to do is start out to do this for you in

simple ways. And let's just try to figure out how many molecules
are there in the substances that we experience in our daily life.
And let's start out with really the most important food, which is
water. How many molecules are there in a glass of water? Here,
imagine a glass of water. And the glass of water that we're
imagining has a volume of about 250 milliliters. That's about a
quarter of a liter. It turns out that water has a density of one
gram per cubic centimeter. That's the density of water. So
therefore, the mass of water in our glass is one gram per cubic
centimeter, times 250 milliliters. A milliliter is the same as a cubic
centimeter. So if we multiply those two numbers, we get the
mass. And that gives us that the mass of water is 250 grams in
our cup. That's the mass.

So how much does a water molecule weigh? Well, this is

something which is known. It turns out that a water molecule is

about 3 times 10 to the minus 23 grams. That is 3 divided by 1
with 23 zeros after it. This is a very small number. But that's the
mass of a water molecule as scientists have determined. So now
if I would like to actually count the number of water molecules
that are in my glass of water, what I do is take my 250 grams
and I divide by the mass of the water molecule, 3 times 10 to the
minus 23. And when I do this, I find that the glass of water has 8
times 10 to the 24 water molecules in it.

That's a huge number. 10 to the 24, that's eight with 24

different zeros after it. That's how big that number is. And that's
the number of water molecules that are in a jar. Scientists
actually love big numbers. The size of the universe is a big
number. If you're a little bacteria, the size of you is even a big
number. But we like use a set of units, which is sort of more
reasonable. And so there is a commonly accepted unit of what we
mean by the typical, large number of molecules that are in a
hunk of stuff. And so it's sort of like if you just take a hunk of
water, how many molecules are in it? And there's a sort of typical
large number that people have agreed upon. And the standard
hunk of stuff, and of course, in order to do this, you have to
decide what hunk of stuff are you going to use. It turns out that
scientists, being somewhat strange people, have decided that the
standard hunk of stuff is going to be 12 grams of the substance
carbon-12.

And so the question is, how many atoms are there in 12

grams of the substance carbon-12? In order to calculate that, of

course, what you have to do is take 12 grams, and then you
divide by the mass of a single carbon-12 atom. And that will give
you the number of molecules. And so that number, it turns out, is
6.022 times 10 to the 23. That's the number of atoms that are in
12 grams of our carbon-12. And that number is given a name.
It's called a mole. A mole is a unit of numbers of molecules that
we will use throughout this class. And one mole is equal to 6.022
times 10 to the 23 molecules or atoms.

So this is a very big moment for us now in this class,

because it turns out that as we've told you, every week in this
class, we're going to have an equation of the week. The equation
of the week is a mathematical equation that typifies, in some
way, one of the main ideas for the week, and allows you to
express it in quantitative terms. So it turns out that this equation,
that one mole is 6.022 times 10 to the 23 molecules, is our first
equation of the week.

Now, in the Harvard College class on science in cooking, we

have over the years adopted a tradition, which is that whenever

the equation of the week is presented, the students, as well as
the professors, must clap. The reason for this tradition is severalfold. It's first to show our appreciation and affection for the
equation, because many people don't have as much affection for
equations as, for example, I do. The second is to emphasize and
really highlight the importance of the equation in expressing the
idea of the week. And in the current context, the idea of the week
really is that one can think about food in scientific terms.

But of course, food is made out of molecules. And the

simplest question that you can ask yourself about the molecular
structure of food is just how many molecules are there. This
equation typifies the typical number that there are. And so now,
without further ado, we should all clap. And I encourage you,
both this week and in subsequent weeks, to follow along at home
and to get in the habit of clapping when we present the equation
of the week.

Now, we could also do the same calculation by starting with

the volume of the molecule instead of with the mass. And for this,
we have to make a simple guess as to what we think the size of a
water molecule is. You could, of course, just go and measure the
size of a water molecule, and use that as your guess. But I want
to just give you a feeling for the orders of magnitudes of things
here. So whereas the last answer I gave you was exactly right,
this answer's going to be a little bit off. But it's more to give you
a flavor of how these things go.

So let's suppose that a water molecule is a few angstroms

across. I don't really know how big it is, but I know that atoms
have a size which is measured in angstroms. One Angstrom is 10
to the minus 10 meters. That's 1 divided by 10 to the 10, which is
1 with 10 zeros after it. This is a very, very small length. I know
that a water molecule is H2O. So there are lots of different
things.

And so let's say, just for the sake of argument, that a water

molecule is about three angstroms in size. So remember, we said

that our glass of water had 250 milliliters, which is the same as
250 cubic centimeters. So the volume of our glass is 250 cubic
centimeters. And I now need to divide by the volume of our
molecule, which I will just approximate is a cube, which is three
angstroms on a side. So I just multiply by 3 times 10 to the
minus 10 cubed. And that's the volume in cubic meters of a water
molecule.

So if you do this calculation, carefully converting between

meters, and cubic centimeters, cubic meters and cubic

centimeters, because I gave you the volume of the liquid in cubic
centimeters and the volume of the water molecule in cubic,
meters, what you find is that this gives you about 9 times 10 to
the 24 molecules in the water. And that's actually very close to
the number we got using it the other way. And that basically tells
you that, in fact, the size of a water molecule is something like
three angstroms on a side, which is very, very small. So the point
is that when you take a macroscopic amount of stuff, like a glass
of water, there is an enormous number of molecules in them. And
that enormous number is basically there because molecules turn
out to be very small.

And so what we're going to do is take the molecules in our

250 milliliters of water, which is 8 times 10 to the 24 molecules.

And we're going to basically ask how many moles is that. Well,
one mole is 6.022 times 10 to the 23. So we simply divide 8
times 10 to the 24 by Avogadro's number. And then that tells us
that actually the number of moles of water that are in 250
milliliters is 13.3. So there are about 13.3. This is an approximate
number. There are 13.3 moles that are in this 250 milliliter glass
of water. And so what that means is if you go, you buy, or you get
yourself a liter of water, a big liter of water, a liter of water
contains four times that, which is about 55 moles. So there are
about 55 moles of water in a liter. That's a definition of the
number of moles that there are in the liter.

Now, one concept that's going to become important as we

go on in this class is the concept of molarity. What we're going to

talk about is, for a given material, we're going to talk about how
many moles are there per unit volume. And a good unit of volume
to use is liters. And so you would talk about how many moles
there are per liter. So for water, we've just said that there are 55
moles of water in one liter. And so we say that means the water is
55 molar. We represent that as 55 capital M.

Moles 2

So if you looked back at how we calculate the number of

molecules of each of the ingredients, the critical number that we

had to give you for you to be able to do this was the number of
grams per mole of each of the different molecules. And actually,
the real difference that gave rise to the number of molecules
becoming more equal, even when the weights were so disparate,
was that the different molecules had different weights. So for
example, water has a molecular weight, we said, of 18 grams per
mole, whereas sugar, that is, sucrose, has a molecular weight of
342 grams per mole. Whereas baking soda, on the other hand,
has a molecular weight of 84 grams per mole.

So it was these different numbers that gave rise to the very

different, numbers of molecules that we found. So now we just

want to take one moment to delve into a little bit more deeply,
where these numbers, where the number of grams per mole of
each species comes from. And it won't surprise you, I hope, to
find out that the answer, again, has to do with molecular
structure. It has to do with the weight of each one of the
molecules individually. And just to make this a little bit more
clear, let's go through and work out some of these weights for
ourselves just so that you can see how those go, and so that you
can get a little bit of context for this sort of thing as we move on
in the course.

So you'll recall that we defined a mole, when we defined

what a mole is, we said a mole is 12 grams of the element

carbon-12, of the isotope of carbon which is called carbon-12.
Now carbon-12 is called carbon-12 because it has within it, six
protons and six neutrons. Protons and neutrons are some of the
elementary constituents of matter, along with electrons. And they
are the ingredients, as it were, that make up the carbon atom.

It turns out the protons and neutrons have a weight which is

about the same as each other, whereas electrons are so much

lighter that when we're thinking about weighing molecules, we
don't have to worry about them at all. Now the weight of a proton
or a neutron is actually a fundamental unit of nature. And it's
given by what scientists call-- there are actually two different
units that are sometimes used by scientists and that we might
use in this course. One is called an atomic mass unit. And the
other is called a Dalton. So an atomic mass unit is equal to
Dalton, is equal to the mass of a proton or a neutron. And in real
units, both of these quantities are equal to 1.66 times 10 to the
minus 27 kilograms. That's a Dalton or an atomic mass unit.

Now carbon-12 has 12 atomic mass units of mass, six

neutrons plus 6 protons. And so that means that the mass of a

carbon-12 is 12 times an atomic mass unit, or about 1.9 times 10
to the minus 26 kilograms. Now if we use the weight method for
counting molecules-- remember, I told you that if you take the
total weight of the stuff that you want to have, and you divide it
by the weight of a single molecule, that will give you the number
of molecules.

Well, if we take 12 grams of carbon-12, and we divide it by

1.9 times 10 to the minus 26 kilograms, we arrive at Avogadro's

number, which is the standard that's used to basically define
Avogadro's number.

So that's carbon-12. So what about water? Well, of course,

water is given by the molecular formula H2O. H is a hydrogen

atom. There are two hydrogen atoms. That's the reason for H2.
And a hydrogen atom basically consists of a single proton. So
then there's O, oxygen. Oxygen consists of eight protons and
eight neutrons. That's 16 atomic mass units, which means that
the molecular weight of water, of an H2O, is 18 atomic mass
units. And if we then convert that to grams per mole, that turns
out to be 18 grams per mole. The 18 came from the number of
atomic mass units that were present in the ingredient in question.

So let's move on and go through some more cooking

materials. So what about sucrose? So sucrose, which is the sugar

that you buy in the grocery store that you cook chocolate chip
cookies with, that is given by the chemical formula C12H22O11.
C12H22O11. So that consists of 12 carbons, 22 hydrogens, and
11 oxygens. Now we already decided that a carbon, this is
carbon-12, consists of 12 atomic mass units. So hydrogen
consists of one atomic mass units and oxygen, we decided,
consists of 16 atomic mass units. So if we want to know the total
number of atomic mass units, what I have to do is count up the
total number in each of these things. So it is 12 times 12. That's
the number of atomic mass units from carbon. That's 144. 22
atomic mass units from hydrogen, and 11 times 16 atomic mass
units from oxygen. Now if we add these all up to each other we
get 342 total atomic mass units. That 342 protons or neutrons
that are present in a molecule of sucrose. And that gives us a
molecular weight of 342 grams per mole.

So you see, the reason that sucrose is so heavy is because

there are just so many protons and neutrons that are in each
molecule.

So we can go on with this and do this for other substances.

So for example just to do one more let's do baking soda. So

baking soda is something we'll come back to and discuss in more
depth later on in this course. But the chemical name of baking
soda is sodium bicarbonate. That has the chemical formula
NaHCO3 -- Na is sodium, H hydrogen, C there's a carbon atom,
and three oxygens. So it turns out that one atom of sodium has a
molecular weight of 23 atomic mass units. Hydrogen is one
atomic mass unit. Carbon, we've already said, is 12 atomic mass
units. And each oxygen is 16. So three times 16 is 48. That's 48
atomic mass units. And if we add them all up, if we add up the
total number of atomic mass units that is in one molecule of
sodium bicarbonate, we get 84. So there are 84 atomic mass
units per molecule, and that means that the molecular weight is
84 grams per mole. And so the origin of the numbers, and, really,
the origin of the different number of molecules in the recipe that
we just talked to is intricately connected to the molecular
structure of the ingredients. And indeed, as you will see, when we
go on with this course, much of cooking and the reactions of
cooking are really connected to the molecules, how many there
are, how they interact with each other, and how we manipulate
them.

So the Nestle Toll House Chocolate Chip Cookie recipe, is my

favorite recipe. And so I really enjoyed being able to count the

number of molecules that were in each of the ingredients. For
your homework this week, one of the things we're going to ask
you to do is that we're going to give you a recipe, and we're
going to ask you to count the number of molecules that are in it.

And I'll just give you a little bit of advice. So you'll notice

that in order to approach each ingredient, I needed to know two

things. First, I needed to know the chemical name and the
chemical formula for the ingredient. So for example, that baking
soda is sodium bicarbonate. And secondly, we needed to know
the molecular weight of each of the pieces of the chemical
formula. So our advice to you is the following, is that you can
always find out the chemical name of something by just googling
it. If you just google the name of an ingredient, it will tell you, oh
that's sodium bicarbonate. Baking soda is sodium bicarbonate.
And it will tell you the chemical formula for that as well. And once
you've got the chemical formula, you can find out the molecular
weight of each of the atoms in the molecule by simply looking at
the periodic table. And then, once you have that, you can put it
all together, calculate the, molecular weight of the ingredients,
and find the number of molecules in your favorite recipe as well.

Chocolate Chip Cookies

Now that we've learned how to count the number of

molecules that there are in a hunk of stuff, in a glass of water,

let's do something more interesting and actually figure out how
many molecules there are in the various ingredients of my
favorite recipe, the Nestle Toll House Chocolate Chip Cookies. So
here, once again, is the recipe for Nestle Toll House Chocolate
Chip Cookies. And although we don't really have time, and you
would get a little bored, if we were to go through and calculate
the number of molecules there are of each of the ingredients,
what I want to do now is start to give you a flavor for this.

And let's start out with what might be the most peculiar of

the ingredients that's in the recipe. At least, if you've cooked it,

you might almost think that you don't need it, but you really do,
which is baking soda. And the recipe calls for one teaspoon of
baking soda. Now, I'm going way ahead of ourselves in this class.
But if you stay with us for another, I don't know, eight weeks or
so, we will tell you why you have to put baking soda in the
cookie. This is a preamble. I'll tell you now. And the reason is
because it turns out that every molecule of the baking soda,
actually, is converted, in the course of the recipe, to a molecule of
carbon dioxide gas, which then tends to puff up the cookie.

So the baking soda is there. It reacts with some of the other

ingredients to puff up the cookie. And you see, the way that I
said this, it was the molecule of baking soda that produced a
molecule of carbon dioxide gas. And so, in a way, you can think
about, in this recipe, the baking soda as putting in carbon dioxide
gas into the recipe. And what really matters here, and you'll see
this when we go forward in this, is the number of molecules.

So now, how many molecules of baking soda are there? So

let's just figure that out. So the recipe calls for one teaspoon of
baking soda. And it turns out that that is about, if you were to
weigh it, five grams. You should make sure your baking soda is
well compacted in your spoon. You know, if it's fluffy, you won't
have as much. And that won't be as good. That's why you really,
when you're cooking, should be weighing your ingredients and
not measuring their volumes. But we won't discuss that very
much now. But anyway, it's 5 grams of baking soda. So it turns
out the molecular weight of baking soda is 84 grams per mole. So
this is the way the molecular weight is reported. And one mole,
that is 6.022 times 10 to 23 molecules of baking soda, the weight
of that is 84 grams. So we therefore can compute the number of
moles of baking soda that there are in this recipe.

We simply take five grams. We divide by 84 grams per mole.

That gives us 0.06 moles. That's the number of moles of baking

soda that's in the recipe. Now, as a number, that's not very
impressive, 0.06 moles. For me, it's actually more impressive if
you just convert it back to the number of molecules, which we
can do, of course, by multiplying by Avogadro's number. 6.022
times 10 to the 23 times 0.06. And it turns out that there are 3.6
times 10 to the 22 molecules of baking soda in this recipe. So
when you make this recipe, you are going to be releasing, if all
the baking soda reacts, about 10 to the 22 molecules of carbon
dioxide gas. And we will come back to the importance of that
later. But that's how much there is.

So now we can go and look at the other ingredients. And

there are lots of other ingredients; so when I'm cooking my batch

of Nestle Toll House Chocolate Chip Cookies, sometimes I decide,
well, I'm not going to put in any salt today. Anyway, the salt
shouldn't matter because it's only asking for about a teaspoon of
salt. How many molecules of salt are you leaving out when you
do that? Well, so it turns out, and you could also look this up,
salt, namely sodium chloride, has a molecular weight which is 58
grams per mole. And you can convert 58 grams per mole. So if
you can simply measure the weight of a teaspoon of salt, you can
therefore compute the number of molecules.

So it turns out the weight of a teaspoon of salt is about 10.6

grams. That's how much it weighs. And if you can simply take
10.6 grams divided by 58, and then you multiply by Avogadro's
number, you find that the number of molecules of salt that's in
the recipe is about 1.1 times 10 to the 23. So there are actually
more molecules of salt in the recipe than there are of baking
soda. Of course, the reason for that is that salt is a smaller
molecule than baking soda. But anyway, that's a lot of salt.

What about sugar? So I don't know about you, but when I'm

making my Nestle Toll House Chocolate Chip Cookies, one of the

most enjoyable parts is filling the cup to 3/4 a cup of both brown
sugar and granulated sugar. There are these two types of sugars.
And we're not going to discuss now why you need them both. But
anyway, so what about sugar? How many molecules of sugar
there are? There's certainly a lot of it that you're pouring in. Well,
it turns out that sugar, granulated sugar, is basically sucrose. And
sucrose has a molecular weight which is 342 grams per mole. It's
actually much heavier than salt. It's about six times heavier than
salt. And so you can also sort of do the conversion and discover
for yourself, that 3/4 a cup of sugar, which is the amount that the
recipe calls for, is about 151 grams. And if you then go and work
out the math, which you should all go and do, right now in your
table, just to check that I'm doing this correctly, it turns out that
the number of molecules of sugar is about 2.6 times 10 to the 23
molecules.

So 2.6 times 10 to the 23 molecules. Now remember, we

decided before there are only about 1.1 times 10 to the 23

molecules of salt. And at least, when I'm doing it, I think, well
gee, the salt is much less important than the sugar. But there's
only a factor of two more sugar molecules in this than salt. And
anyway, I don't know about your chocolate chip cookies. But
when I make mine, they taste sweet. They don't actually taste
salty, even though you're actually putting quite a bit of salt in the
recipe. That's also an interesting thing.

So one can go through a similar conversion for other

ingredients. So brown sugar, which is very related to sugar. There

are a couple of other ingredients. It turns out that it's about 2.4
times 10 to the 23 molecules of brown sugar. What about
protein? We all talk about protein. How many protein molecules
are there in this recipe? Well, if you look through the various
ingredients, there are various places where protein comes in.
Protein comes in in the egg. Remember, we already talked about
ovalbumin. Another place that protein comes in is in the flour.
Gluten, which is actually one of the major constituents of flour, is
itself a protein. Let's, just for fun, we could go through this in
much more detail, but, let's just count the number of proteins
and molecules there are in an egg.

And actually, I'm going to simplify this dramatically because

eggs are rather complicated things. There are lots of different

protein types in them. But one egg, it turns out, contains within
it, if you just go look at a food label or something for egg, one
egg contains about four grams of protein. So this recipe calls for
2 eggs, which is about 8 grams total. And we now have to figure
out how many protein molecules there are. And so what I'm
going to do is very simple-minded, but it should at least give us
the right number, is I'm going to take one of the major
constituent proteins in egg. I'm going to take a protein called
ovalbumin, which is a major protein component of egg white. And
it turns out that an ovalbumin p protein weighs, each one, which
is, remember, a long chain of amino acids, we talked about this
before, each molecule weighs about 7 times 10 to the minus 23
grams.

So if you then take the 8 grams, which is the total protein

content, and you divide by 7 times 10 to the minus 23, just

assuming that the protein is ovalbumin, that gives us about 1.1
times 10 to the 23 protein molecules. So actually, there are as
many molecules of protein, at least in the egg, as there are
molecules of salt. So even though they have widely different size,
actually, the number of molecules is not so different. So let's just
do one more for fun. And then I'll show you a summary.

So another thing this recipe calls for, which I usually include

when I cook the recipe, I don't know if you always do, but it's a
small ingredient that one might tend to neglect, is the vanilla
extract. And the recipe calls for one teaspoon of a vanilla extract,
which is about four grams. Now, it turns out, that the main
ingredient of vanilla extract, which, of course, is a flavor molecule
which is there to give the cookie a taste of vanilla, is as a
molecule called vanillin. Creative name, vanillin. And it turns out
the vanillin has a molecular weight of about 151 grams per mole.
That's the molecular weight of vanillin. And if one goes through
the math that I've been describing, and you should all, of course,
check me on this, the number of vanillin molecules that there are
in the vanilla extract is about 1.5 times 10 to the 22.

So again, the number of molecules of the vanillin is not so

much smaller than the number of molecules of everything else.

They're all basically within a factor of 10 of each other, all of the
different molecules in this recipe. We can go through this and do
this for other ingredients. We could take flour. That turns out to
be about 300 or so grams. And when one computes the number
of molecules from this, it turns out it's about 6 times 10 to the 20
molecules of the starch molecules in flour. These are long
molecules, remember I said, but still that's a number which is
actually lower than the other number when one looks at it in
terms of molecules. Of course there's so much flour because
these molecules are much bigger.

So now, just to summarize, and one can do this for all of the

other components too, and I think that this is a really very

interesting way of looking at the different ingredients within the
Nestle Toll House Chocolate Chip Cookie recipe, which might give
you a different feeling for it than you have when you just look at
the ingredients from scratch, the largest number that at least I
was able to find in my quick summary through them turns out to
be that in the fat from butter. One of the main compounds is
called butyric acid. And it turns out that there are about 1.6 times
10 to the 24 molecules from that. There are about 2.65 times 10
to the 23 molecules of granulated sugar, and so on, and so forth.

And this is a list of ingredients of the Nestle Toll House

Chocolate Chip Cookies which is shown in a different way. And of

course, it raises many questions which, hopefully, you will now
start to think about. How do these molecules interact with each
other? Why are the numbers, the different ratios, what they are?
And how do they actually get together to build the architecture of
what we think of as being the perfect Nestle Toll House Chocolate
Chip Cookie?

pH

o Ferran, talked about a glass of water, and Michael just told

us about how many moles and molecules there are in a glass of

water. And water, of course, is very good for you. But for the
purposes of this segment, I'm going to make it a little bit more
interesting, and make water a little bit more delicious by adding
some lemon and some sugar. So we're going to make lemonade.

So here's a recipe for lemonade. So if you take six lemons,

five cups of water and sugar, you add it all together in a pitcher,
you stir, you serve it over ice, and there you have lemonade.
Lemons, of course, are the perfect example of something we
think of as being very, very sour. And in fact, a lot of foods, when
they have a sour taste to them, it's usually caused by an acid.
And in the case of lemons, the acid is citric acid. In the case of
apples, one of the main acids is malic acid. And there's a whole
host of other common organic acids, that are such things as
tartaric acid, benzoic acid, ascorbic acid, and so on. And that's
usually what's giving the sour taste of foods.

Citric acid is a weak acid, as opposed to other, stronger acids

you may have heard of such as sulfuric acid, which you use in car
batteries. And a lot of organic acids are weaker acids. So what is
an acid? An acid is, by definition, a molecule that releases a
hydrogen ion. And so here is an image of citric acid releasing a
hydrogen ion. And the measure of how strong an acid is, is a
measure of how easily an acid gives up that hydrogen ion. And
so, for example, citric acid gives up the hydrogen ion not as
easily as, say, sulfuric acid does, which we use in car batteries.

In this lemonade, what happens when the citric acid is

added? So what happens, is that the citric acid releases the

hydrogen. The hydrogen doesn't easily float around on its own.
But there's a lot of water molecules around in the water that we
added to the lemonade. And the hydrogen ion is taken up by the
water, and it's giving us -- instead of an H2O, it's giving us an
H3O+, and this is usually referred to as a hydronium ion. So how
acidic something is, then, is a measure of how easily hydrogen
ions, are given off. And we usually also refer to hydrogen ions as
protons. And the more hydrogen ions and, indirectly, how many
hydronium ions, there are around, is what gives us a measure of
how acidic something is.

So it turns out that the number of hydrogen ions in water

naturally is 10 to the power of negative 7 moles per liter. And so

Michael just told us that in a glass of water, in a liter of water in
fact, there are 55 moles of molecules per liter. And so 10 to the
negative 7 then, is actually a very, very tiny amount. But
nevertheless, this is how many hydrogen ions there are in water.

Water is thought of as being neutral, and acids are

molecules that easily give up hydrogen ions, and so they're

acidic. And so then at the other end of the spectrum, we have
molecules that are very, very reluctant to give up hydrogen ions,
even more so than water. And those we think of as bases, or
basic molecules. And another way to think of them is as
molecules that very easily take up the hydrogen from acids such
as citric acid or so on.

So of course 10 to the negative 7 is a very tiny number. And

it's kind of clumsy, even to say. So scientists have thought of a

way to express this more easily. And there is a mathematical
formula for this, which is pH equals minus the logarithm of how
many moles per liter of hydrogen ions we have. And so if we do
this for water, where we know that the number of hydrogen ions
is 10 to the negative 7, and we plug this into this formula, we
say, minus the logarithm of 10 to the negative 7. And for those of
you who are comfortable with logarithms, you immediately see
that the answer to this is 7. And if you're not, you can plug this
into your calculator and actually see that the number for this is 7.
And so the pH of water is 7. And this is something that a lot of us
are very familiar with, and if not, this is a good reminder.

Here's a glass of water, so let's actually measure the pH and

just make sure we're on the right track. So there are these pH
strips which you can buy, and they're fun things to have around
the house, because you can run around and measure the pH of
everything. So let's measure the pH of water. And you'll just stick
the stick in like this, and then the color changes, on the pH strip.
And you compare it to the color on this box, and it turns out that
the pH is 7. So that's good.

Here is some lemonade. And I was lazy, so I bought some

lemonade. Now we can compare this to our calculations. So the

pH of this - you dip it down, and you can see already that the
color is very different. And we can compare it to our box. And I
would say that that's approximately a pH of 2. Here, by
comparison, I have a lemon. So let's just compare the pH of this
to our lemonade. And I'll just do that by dipping this pH strip in
the lemon juice -- try to get some liquid on there. And then we
can compare, and the pH is actually -- it's a little bit more sour,
but it's not that much more sour than the lemonade. But
lemonade just on its own, even with water is also very, very
acidic. So the pH of the lemonade, we found, was 2.

And if we now use our equation, we can find out how many

hydrogen ions that corresponds to. And so we can solve for the
number of hydrogen ions, and if we do that, we find that the
number of hydrogen ions is equal to 10 to the power of negative
pH. And if we plug that in, the number of hydrogen ions is 10 to
the negative 2 moles per liter, so a lot higher than that for water.
And if you compare the water with the lemonade, you find that
there is five orders of magnitude more hydrogen ions in
lemonade than in water.

And in fact, this is a very important point with pH in general.

So the difference in concentration of hydrogen ions -- if you

compare pH 4 to pH 5, is a tenfold difference. And so if you
compare pH 3 to pH 5, there is a hundredfold difference.

Here is a chart of many common beverages that we see in

our everyday lives. And you can see where all of them fall on the
pH scale. So water has a pH of 7, lemon juice has a pH of 2,
orange juice a pH of about 3. Baking soda is basic, and so has a
pH of 9, and so on. And so if you want to do something fun, go
around in your home and measure the pH of a lot of different
foods. And you can now calculate how many hydrogen ions that
corresponds to.

And what you'll probably find is that foods that have a lower

pH tend to taste more sour and this is because the acidity is very
closely related to what we experience as sour. Now an important
note is that taste is something that scientists are still learning a
lot about, and our taste buds actually do not detect the hydrogen
ions. They detect the molecule as a whole. And so the sourness of
something is an indication of how acidic something is, of how low
the pH is, but it's not directly correlated.

So let's go back now to our recipe for lemonade. And we can

calculate how acidic the lemonade should actually turn out,

according to what we now know about pH. So six lemons -usually you think of a lemon as corresponding to about three
tablespoons of lemon juice. And this then corresponds to 270
milliliters, which is 0.27 liters of lemon juice. We know that the
pH of lemon juice is 2. We also know that five cups of water
corresponds to 1.2 liters of water, and so if we now calculate how
many hydrogen ions there are in each of these, and then we
divide by the total volume, we'll find how many moles there are
in a liter, and we will find the pH of the lemonade. So if we now
plug this in, we get 0.27 liters times 10 to the negative 7 moles
per liter, plus 1.2 liters times 10 to the negative 7 moles per liter
over the total volume which is 1.2 liters plus 0.27 liters. So this
equals 0.0018 moles per liter. And if we now plug this into our
equation again, and the equation is pH equals the negative
logarithm of the number of moles per liter, we find that the pH is
2.7.

So what you can do to analyze this is you can make a

number of different lemonades, or you can buy a number of

different lemonades, and find what your favorite pH of lemonade
is. And next time you share the recipe for that lemonade with a
friend, you can say instead of just giving how many lemons and
how much water you're supposed to add, you can just say mix
lemon juice and water to a pH of 2.7, stir, and serve over ice.

So to wrap up, acids of course are important in cooking, not

just for taste but for a lot of other things. For example when we
cook ceviche, we marinate it in lemon juice and it's the acidity
that is causing the denaturation of protein that cooks the fish.
And when we make ricotta cheese, it is the addition of vinegar
and heat that causes the cheese to form. And additionally,
reactions between acids and bases are very important for baking.
And there are many other reactions in cooking, such as Maillard
reactions or browning reactions that are also dependent on the
pH.

28/11/2013 13:09:00

Calculating how to cook a perfect egg

At home sous vide eggs

Materials:

1 stove or hot plate

2 pots, medium to large in size OR 1 pot and 1 kettle

1 thermometer

1 or more bowls (for cracking eggs into)

Tongs, spoon, or similar utensil for removing eggs from hot

water

Ingredients:

12 eggs (room temperature)

Water

Procedure:

If the eggs are in the fridge, set them out to warm up to

room temperature before continuing. Starting with cold eggs will

make the process take longer.

Fill one of the pots with water. Place three eggs in the water

(they should be covered by about 1 inch of water) and bring to a

boil. Once a boil is reached, turn off the heat and cook the eggs
for 10-15 minutes. Remove the eggs and set aside to cool. Do
NOT discard the water it will be used in the next step.

Fill the other pot or kettle with water and bring to a boil.

Measure the temperature of the water bath left over from

part 2. If it is greater than 62C, let it cool until it reaches this

point. If it is lower than 62C, add boiling water until it reaches
this temperature.

Place three eggs in this 62C bath. Keep this bath between

58C and 62C for at least 20 minutes (30-40 if possible) by

adding boiling water to the bath as it loses heat to the eggs and
the surroundings. The temperature range doesnt need to be
perfect, but ideally the bath should not sit above 62C for more
than a few seconds at any given point in time. The target
temperature for the final eggs will be the average of the upper
and lower limits (60C). It might be helpful to note how long on
average it takes for the water bath to drop one degree so that
you dont have to monitor the temperature of the bath constantly
(the time will vary based on a number of factors, but a good
starting estimate would be that 1 degree is lost every 1.5
minutes).

After enough time has elapsed (at least 20 min, but ideally
30-40 min), remove one egg from the bath, carefully run under
cold water in the sink, and crack the egg into a bowl. If it looks to
be the appropriate consistency given Dave Arnolds demonstration
in the lecture material for the week, take the other two eggs out
as well and set them aside. If not, leave the remaining eggs in
the bath for another 10 and 20 minutes, respectively, and repeat
step 5.

Repeat steps 5 and 6 using a water bath in the range of 61-

65C and a bath in the range of 64-68C in order to obtain eggs

at a final temperature of 63 and 66C, respectively.

For each of the temperature ranges, estimate the internal

temperature of the egg by comparing the doneness of the egg to
the consistencies described by Dave Arnold in his video on Sous
Vide eggs.

For credit on the lab, click ahead to the end of the lab

section and describe your experiment in a brief lab report.

28/11/2013 13:09:00

Hollandaise sauce is a classic French sauce often served with

fish or vegetables. The following is Julia Child's recipe from Julia

and Jacques Cooking at Home.
1 Tbsp. water
1 Tbsp. fresh lemon juice
3 large egg yolks
6-8 oz. very soft unsalted butter
1 dash cayenne pepper
+ salt and ground white pepper to taste

Whisk the yolks, water, and lemon juice in the saucepan

until thick and pale.

Set the pan over moderately low heat and continue to whisk

at reasonable speed, reaching all over the bottom and insides of

the pan, where the eggs tend to overcook.

Frequently move the pan off the burner for a few seconds,

and then back on. (If, by chance, the eggs seem to be cooking
too fast, set the pan in the bowl of cold water to cool the bottom,
then continue).

As they cook, the eggs will become frothy and increase in

volume. When you can see the pan bottom through the streaks of
the whisk, remove from the heat.

By spoonfuls, add the soft butter, whisking constantly to

incorporate each addition. As the emulsion forms, you may add

the butter in slightly larger amounts, always whisking until fully
absorbed. Continue adding butter until the sauce has thickened to
the desired consistency.

Season lightly with salt, pepper, and a dash of cayenne

pepper, whisking in well. Taste and adjust the seasoning, adding

droplets of lemon juice if needed. Serve lukewarm.

Answer the following questions about Hollandaise, a fat-in-

water emulsion.

MAYONNAISE

Materials:
mortar & pestle OR a medium bowl with a whisk or fork
Second bowl (for collecting the egg white)
1 small pot (if using garlic)
1 cutting board (if using garlic)
1 knife (if using garlic)

Ingredients:

1 egg yolk
olive oil (or any other type of oil)
salt & black pepper
Optional: 1 clove garlic
Optional: tsp mustard

Procedure:

1. Separate the egg yolk from the egg white. This can be

done by simply cracking the egg into your hand over a bowl and
allowing the white to run through your fingers while carefully
keeping the yolk from falling through or breaking. Set aside the
egg white for Part II.

2. Before you start, weigh the egg yolk and calculate its

volume using the density given on the worksheet.

3. If you decide to make mayonnaise with garlic:

a. Peel the garlic and place in the pot. Cover with cold water

and place on the stove. Bring the water to a boil, then drain the
garlic and cool in cold water.

b. Chop the garlic into medium-sized pieces, place the

pieces in the mortar, and add 2g of salt.

c. Thoroughly mash the garlic using the mortar and pestle.

The garlic should become a smooth paste.

d. Add the egg yolk and mix everything with the pestle. Go

to step 6.

4. If you decide to make mayonnaise with mustard:

a. Add the egg yolk and a teaspoon of mustard to the

mortar and mix with the pestle. Go to step 6.

5. If you decide to make simple mayonnaise:

a. Add the egg yolk to the mortar and mix with the pestle.

Go to step 6.

6. Measure out about 30 ml of oil. When your mayonnaise is

done you want to be able to calculate how much olive oil you
have added, so you will have to measure the final volume and
subtract it from this initial volume.

7. Drizzle oil very, very slowly into the bowl or mortar while

continuously whisking or grinding with the pestle. If you add oil

too fast the emulsion will break and then it cannot be saved. If
you are making the mayonnaise with someone else, this is best
done with one person adding the oil slowly while the other person
mixes.

8. When you have a reasonable amount of stable emulsion

(you should be able to hear a very loud smacking sound and the
emulsion should be stiff enough that it wont fall out of the bowl
easily if flipped upside down), measure the volume of the
remaining oil and calculate roughly how much oil you have used.
Next, use your measurement to calculate the volume fraction of
the mayonnaise. Record this number in the lab report for credit.

9. Add salt and freshly ground black pepper to taste, and

enjoy with bread or vegetables while continuing to the next step!

NANDU JUBANY: Well make now another emulsion, a

prawn in hollandaise sauce. It is also an emulsion and well
make it with egg yolk and hot butter, in this case prawn butter.

We have sauted the prawns heads with garlic and a little

bit of chili pepper and we added the butter. We let it make an
infusion. We have put it here to make the emulsion. Good, well
take the same, in this case well use 2 egg yolks, well use 2
egg yolks to make the emulsion easier. Nothing else well do the
trick - it is a good trick, I love it.

And well whisk the eggs well put the eggs in a double

boiler like this. Its very important, like with the alioli, it will
separate for two reasons: changes in the temperature I mean,
the egg yolk has to be at the same temperature that the prawn
butter, if not, it will separate. Well always have the hot water
trick -- here I have a little hot water in case I need to use it.

It starts to have temperature, and well add a teaspoon of

water. We are emulsifying the egg yolk, we turn off the fire, we
keep emulsifying. It is very important having a well done
emulsion, if the egg yolk is not at the same temperature it is not
worth to beginning with the emulsion because it will separate.
Obviously there must be a balance between the butter and the
egg yolk, its the balance between the water and the fat. Look,
we already have it, and we have the same temperature here and
in the butter. Well add a drop of water because its still very
thick, and we start adding the butter like this.

Its very important to have the same temperature. Look,

this is the moment, look. It is very thick, well add a drop of

water and after this, the final trick, and we could not add the
buttermilk. At the bottom, we have this, that is the buttermilk,
we could reserve this part and not add it. This part is like water,
but it tastes like prawn and it tastes like butter also, so Im
going to add it, and it will do the effect of the water it will help us
finally. Its going to be perfect. Well mix it a little and we add
it. We add it all. Since we have the texture we want,

Like this well have a perfect sauce. We have put 2 egg

yolks because we want the sauce to cook au gratin and we add it

all. We have finished the emulsion. We are going to add parsley
or tarragon, in this case I choose parsley. And the emulsion is
ready. We can now add salt, pepper, or whatever, and well finish
the dish.

To finish the dish we have prepared some grilled prawns

from Palams, underdone, fried round potatoes, and raw, sliced

mushrooms, and we have reserved the coral.

We have the hollandaise sauce which we still need to fix.

Well add more salt, a bit of tarragon, vinegar, just a few drops.
We could have fixed it before, but now is ok, and a bit of white
pepper.

I think it will be very good. We already have it, we are going

to place it on a plate.

-Hello

- Hola

- Well, we have the hollandaise sauce ready, and we are

going to serve the plate.

- Is this parsley from your garden?

- yes, the prawn, the juice, also potato balls, and now it is

mushroom season 4 mushrooms, and here we have the head

prawns juice to end Well put the hollandaise sauce

- Wow, that looks wonderful.

- Mm, very good. So what do you keep an eye on to make

sure the emulsions doesn't break?

- A little bit of water in the right moment.

- And so the water is hot?

- Yes, hot hot..

-And so it's the water and the temperature, and the

surfactants in the egg?

-Well, when its absolutely separate, theres nothing we

can do, we need to start again.

-Would you like to try it?

-Yes, I'd love to.

-The prawn

-Mm, it's really good.

-Thank you so much

-What is this?

-Potato, fried potato, special potato.

-We could au gratin this dish because of the egg yolk.

Is it good?

-Beautiful, delicious.

28/11/2013 13:09:00

NANDU JUBANY: This is a traditional alioli recipe. Traditional,

as we use to eat it nowadays, the real traditional alioli would be

only with garlic and olive oil. Here we are going to make a trap,
and we'll add egg yolk. This egg yolk is used so that we can put
less garlic. We do that because in this way we can eat more. I like
when I eat lamb or whatever if I can eat more alioli.

We take a garlic clove and we take out the inside part and

put it into the mortar. For one egg yolk we'll use two garlic cloves.
We open it and it's ready. It is important to put a little salt to the
garlic, so it does not jump out. We need to mash the garlic cloves
until we get a paste. If we had not put salt, the garlic cloves
would be jumping out. It is very important to add salt because of
this, and so we don't need to add it again.

We'll take the egg, and this is a trick, see we have the egg

yolk inside. We add the yolk here, you didn't know about this
trick, did you? And we can start now, you can help yourself, with
a little hot water, a few drops of hot water when necessary.

We'll start to whisk the eggs. A good virgin olive oil, with low

acidity, only 0.4 degrees of acidity. Here we have a Siurana, a

Catalan olive oil. And we'll start, first we'll start very slow, and
after a while we'll keep whisking. Now we can add a few drops of
hot water, only a few.

It's very important, in the emulsion, to have the same

temperature between the egg yolk and the oil. It's really
important. If we don't have the same temperature, it'll separate.
If the egg is in the fridge and the oil is outside, it'll separate for
sure.

Here we have the same temperature. We have to be careful

at the beginning. After, it is more difficult to separate. In a

moment it'll start to make a sound, the alioli. Here we call it
trincar. It's the sound you are listening for. This noise means that
we are doing a good job, the emulsion is perfect. I believe it's
going to be ok now. It's still thick, but we need to keep doing it
because it has a lot of garlic taste still. Now we'll add a few drops
of hot water.

There are some people who add a few drops of lemon, but I

believe that alioli is without lemon. This noise means we are

doing great. We almost have it. Now we have a perfect alioli. Let's
see how salty it is a little more saltAnd we have it. We have it.
To know if it's very thick, there is a way that is to turn the mortar.
Here we have a good emulsion, see, a perfect emulsion. And very
tasty.

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