PROTEINS

Unit-IV
Proteins
* Classification
* Caloric value
* Recommended daily allowances
* Dietary sources
* Functions
* Digestion, absorption, metabolism and storage
* Malnutrition: Deficiencies and Over consumption

INTRODUCTION

Protein first importance

Greatest

importance in nutrition
Very important macronutrient
Forms the main basic unit for body cells
Body building nutrient primary function
Source of energy in absence of CHO & Fat

 Complex

organic nitrogenous compounds

Composed of carbon, hydrogen, oxygen, nitrogen,
& sulphur varying amounts
Some proteins also contain phosphorus & iron &
occasionally other elements
Constitute about 20 % of the body weight in an
adult

 AA

the basic unit of Protein

Several amino acid combines together to form
protein
Protein

compound of high molecular weight, in

which number of AA join through peptide bond to
form polypeptide chain called protein

AMINO ACID
Smallest

unit of protein
It is nitrogenous compound
Having, carboxyl group COOH & amino NH2
group

ESSENTIAL AMINO ACIDS

 Proteins

are made up of smaller units amino acids

20 AA are stated to be needed by the human body
8 are called essential
because the body cannot synthesize them in
amounts corresponding to its needs
Therefore, they must be obtained from dietary
proteins

Non EAA
1.
2.
3.
4.
5.
6.
7.
8.
9.
10.
11.

Alanine
Arginine
Asparagine
Aspartic acid
Cysteine
Glutamine
Glutamic acid
Glycine
Proline
Serine
Tyrosine

EAA
1.
2.
3.
4.
5.
6.
7.
8.
9.

Leucine
Isoleucine
Lysine
Methionine
Phenylalanine
Threonine
Valine
Tryptophan
Histidine-evidence-essential

 Both

EAA & non EAA are needed for synthesis of

tissue proteins
EAA must be supplied through diet
Non EAA synthesized by the body provided
other building blocks are present

Biological functions
Formation

of niacin from tryptophan

The action of methionine as a donor of methyl
groups for the synthesis of choline, folates &
nucleic acids
Cystine & throsine are essential for premature
babies
New tissue cannot be formed unless all the EAA
are present in the diet

protein is said to be biologically complete if

it contains all the EAA in amounts corresponding
to human needs

When

one or more of the EAA are lacking, the

protein is said to be biologically incomplete

 Animal

proteins rated superior to vegetable

proteins
Animal proteins biologically complete
Ex- milk & egg proteins

Classification

CLASSIFICATION OF PROTEINS
ON BASIS OF
SHAPE

ON BASIS OF
COMPOSITION

ON BASIS
OF
ORIGIN
Plant

ON BASIS OF
QUALITY

Globular

Simple/holo

Complete

fibrous

Conjugated/complex Animal

Partially complete

Derived

Incomplete
High biological value
Low biological value

Classification on basis of shape

Globular protein
These proteins are spherical in shape & play role
in variety of biological function
Ex:
blood protein like serum albumin,
glycoprotein, antibodies, heamoglobin, hormones,
enzymes

Fibrous protein
These have long ribbons of fibre like structure
It is mainly found in animal body
It is fully or partially resistant to action of
enzymes
Ex: protein of skin, hair, nails

Classification on basis of composition

Simple or holoprotein
It

possesses only amino acid in their structure

Ex: albumins, globulins, glutelins, prolamine,
scleroprotein or animal skeleton protein

Conjugated or complex protein

These

protein possess non protein component

called prosthetic group along with amino acid in
their structure
Ex: haemoglobin, glycoprotein & nucleoprotein

Derived protein
Obtained

as a result of treatment of simple or

conjugated protein with heat, enzymes or
chemical
Ex: peptones and polypeptides

Classification on basis of origin

Animal
Plant

protein

protein

Classification on basis of nutritional

quality/essentiality - AA
Quality

of protein depends on types of AA in their

structure & their composition

Essential or complete AA
Cannot

be synthesized by body itself

To be consumed in diet by humans

Partially complete or conditionally EAA

Some AA-

which are not synthesized in infants,

while adults can synthesise it
Essential for one particular group
Ex: arginine intestinal metabolic dysfunction
Cystein, glycine, proline, tyrosine

Incomplete or non EAA

Body

can synthesize itself

Not necessary to be present in diet

High biological value protein or complete protein

Protein

which contains all EAA in their structure

Animal sources

Low biological value protein

Usually

obtained from plant sources

Protein deficient in one or more of the EAA
Ex: maize tryptophan is limiting, lysine absent
in wheat

Caloric value

kcal of energy / gram

Tissue

building
Inadequate CHO & fats

Recommended daily
allowances

RDA
Depends

on the type of protein being consumed in diet

High biological value protein animal origin
requirement is less
Generally, 1 gm per kg body weight for adults - ICMR
Requirement changes with age & physiological
condition
Infancy, childhood, adolescent, pregnancy & lactation
requirements are high

GROUP

PROTEIN GM / DAY

Man

60

Woman

50

Pregnant woman

50+15

Lactation
0-6 month
6-12 month

50+25
50+18

Infancy
0-6 month
6-12 month

2.05 / kg
1.65 / kg

Children
1-3 years
4-6 years
7-9 years

22
30
41

Boys
10-12 years
13-15 years
16-18 years

54
70
78

Girls
10-12 years
13-15 years
16-18 years

57
65
63

Dietary sources

 Animal

sources
Vegetable sources

Animal sources these contain all EAA

Milk
Meat
Eggs
Cheese
Fish
Fowl

 These

proteins contain all the EAA in adequate

amounts
Egg proteins are considered to be the best among
food proteins
because high biological value & digestability
They are used in nutrition studies as a reference
protein

Vegetable sources
Pulses (legumes)
Cereals
Beans
Nuts
Oil seed cakes

 Vegetable

sources are poor in EAA

Cereals & pulses main sources of dietary
protein
They are cheap, easily available, consumed in
bulk

Protein contents of some foods

FOOD

PROTEIN (gm. Per 100 gm of food)

Animal foods
Milk

3.2-4.3

Meat

18.0-26.0

Egg

13.0

Fish

15.0-23.0

Plant foods
Cereals

6-13

Pulses

21-28

Vegetables

1-4

Fruits

1-3

Nuts

4.5-29

Soyabean

43.2

Others
Oils & fats

Nil

Sugar & jaggery

Nil

Supplementary action of proteins

Cereal

proteins- deficient in lysine, threonine

Pulse protein-methionine
When 2 or more of vegetarian foods eaten
together
Proteins supplement one another & provide a
protein comparable to animal protein
Vegetarian- high grade protein , at low cost

Functions

Growth and development

Basic cell building material
New cell formation
Repair of damage tissue
Ex:

collagen

Enzymes & co-enzymes

Catalyse metabolic reaction are proteinous in
nature
Ex: urease, amylase, catalase, cytochrome

Hormones formation
Hormones play regulatory role in several
metabolic function of cells
Ex: epinephrine derived from AA tyrosine

Transport or carrier protein

Several protein acts as carrier of essential
biological factors to various parts of organism
Ex: globin - a protein acts as carrier of it heme
i.e iron in body & haemoglobin which acts as
transporter of oxygen in the body

Visual pigments
The visual pigment which enables us to see are
protein in nature
Rhodopsin of rod cell & iodopsin of cone cells of
retina are protein

Contractile protein
Ability to move & contract in animal is also
provided by certain specific protein
Example: muscle protein actin & myosin make
muscle fibre contractile

Defence protein
There are certain special protein which increases
our immunity
They defend human body against foreign material
Ex: anti bodies, interferon which are antiviral in
nature

Toxin
Some protein are toxic in nature & proves to be
vulnerable on entering in human body
Ex: snake venom

Regulatory protein
Protein plays role in regulating physiological
activity
Ex: insulin regulates sugar metabolism

Fuel
Protein can also provide energy
When CHO & fat are deficient in diet

Biological buffers
Protein helps in maintaining acidity & alkalinity
of cell, so act as biological buffers

Storage protein
Some protein acts as storage protein
Ex: albumin of egg & gluten of grain

Digestion, absorption, metabolism

and storage

Digestion

 The

digestion and absorption of proteins is

very efficient in healthy humans, hence very
little protein (about 5-10 g/day) is lost through
feces

 Proteins

are too large to be absorbed.

The dietary proteins are hydrolyzed to amino acids
by proteolytic enzymes, which can be easily
absorbed.
Proteolytic enzymes responsible for degrading
proteins are produced by three different organs;
The

stomach, pancreas and the small intestine.

Protein Digestion
Proteins

are broken down to

Tripeptides
Dipeptides
Free amino acids

Peptide
bonds
Ami
no
acid

Ami
no
acid

Ami
no
acid

Amin
o
acid

Amin
o
acid

61

Peptide
bonds
Ami
no
acid

Amin
o
acid

Ami
no
acid

Ami
no
acid

Amin
o
acid

Amin
o
acid

Amin
o
acid
Amin
o
acid

Amin
o
acid

Amin
o
acid

62

 The

hydrolysis of complex protein takes place in

several steps

Ultimately

form

get converted into simple absorbable

Characteristics of proteolytic enzymes

They

are hydrolases.
Secreted in the zymogen (Inactive) form, converted
to active form in the intestinal lumen.
The active site of the enzyme is masked by a small
region of the peptide chain that is removed by
hydrolysis of a specific peptide bond.

Characteristics of proteolytic enzymes

They

may be Exopeptidases or Endopeptidases.

Exopeptidases catalyze the hydrolysis of peptide
bonds, one at a time, from the ends of peptides.
Endopeptidases hydrolyze peptide bonds between
specific amino acids throughout the molecule.

Steps
Mouth

or buccal cavity
Gastric phase
Intestinal phase

Proteolytic enzymes of GIT are

secreted by three different organs

67

Mouth
No

protein digesting enzyme

No protein digestion
Lubricates food to help in swallowing
this helps in making food soluble for the action of
proteolytic enzymes.
After mastication and chewing, the bolus of food
enters stomach where it is acted upon by gastric
juice.

Gastric phase
Protein

undergoes both mechanical and chemical

changes
Stomach contains gastric juice HCl &
2 protein digesting proenzymes
Pepsinogen or propepsin &
prorenin

First
HCl
Pepsinogen

Pepsin

HCl
Prorenin

Renin

Later ,
Pepsin
Pepsinogen (inactivated)
Pepsin
Pepsin

Pepsin

- carryout protein digestion

convert protein to proteoses ( partially

hydrolysed product)

Digestion of protein begins

in the stomach

72

Renin
Protein casein
(milk protein)

Paracasein + Whey Protein

*Whey protein is a mixture of gobular proteins isolated

from whey,
the liquid material created as a by-product of cheese
production

Paracasein + Calcium

Calcium Paracaseinate

Pepsin
Calcium Paracaseinate

Peptones

76

Intestinal Phase
Pancreatic

juice contain various inactivated protein

digesting enzymes

Chymotrypsinogen
Procarboxy

peptidase
Trypsinogen
Various

protein splitting enzyme are secreted in inactive

forms to protect cells protein

 The

proteolytic enzymes present in pancreatic

juice are:
Trypsin
Chymotrypsin
Elastase
Collagenase
Carboxypeptidases

 Enzymes

present in intestinal juice are:

-Enterokinase
-Amino peptidases
-Prolidase
-Di and Tri peptidases

Enterokinase
Trypsinogen

Trypsin

Trypsin acts as autocatalyst

Trypsin
Trypsinogen

Trypsin

Trypsin acts upon protein & other

proenzymes to form protein & active
protein digesting enzymes

Trypsin
Protein

Peptides
Trypsin

Chymotrypsinogen
Trypsin
Procarboxypeptidase

chymotrypsin

Carboxypeptidase

Carboxypeptidase
Peptides

Dipeptide + Amino acid

 Intestinal

juice contain 2 protein digesting

enzymes
Amino

peptidases
dipeptidases

Aminopeptidases
Peptides

Amino acid + Dipeptide

Dipeptidases
Dipeptide

Amino acid

Role of Elastase and Collagenase

Elastase
Activated by Trypsin
Has maximum activity on peptide bonds
contributed by carbonyl groups of neutral aliphatic
amino acids- Alanine, Glycine, Serine etc.
Collagenase- Acts

on Collagen

Absorption

 Proteins

are completely digested to constituent amino

acids.
But some amounts of oligopeptides may remain
undigested.
The products of digestion are rapidly absorbed.
Site of Absorption- Oligopeptides are absorbed from
duodenum. and proximal Jejunum,
while amino acids are absorbed from ileum and distal
jejunum .

Mechanism of Absorption
The

absorption takes place by active transport (same as that

of glucose).
Vitamin B6 is involved in the active transfer of amino
acids.
Energy requiring process, ATP is required as a source of
energy
A carrier protein is also required which may be Na+
dependent or independent.
Different carrier proteins are there specific for different
amino acids.

Absorption of amino acids

By Na+ dependent active transport system

(Na+ amino acid cotransport)
An energy requiring process
There are 5 different
carriers for amino acids
Transporter for acidic amino acids
Transporter for basic amino acids
Transporter for neutral amino acids
Transporter for amino acid
Transporter for - amino acids

91

Metabolism

 AA after
Firstly

absorption has various fate

reaches via hepatic portal vein into the

liver
In

liver protein is released by liver to body cell to

cell of body material formation

 Other

surplus AA combines with CO2 to form

urea CO (NH2)2

This

urea is excreted out through urine

Some

AA converted to sugar or fat to give energy

especially in fasting

AMINO ACID

LIVER

Protein released by liver to

body cell

Protein

Surplus AA

Converts
Sugar or Fat

Participate in body building

& maintaining function

Combines with CO2

CO (NH2)2
Energy

Excreted out
Urine

Storage

 Extra
So,

protein is converted into fats & carbohydrates

there is no specific protein storage site &

storage form of protein

Malnutrition

Deficiencies

Over consumption