Protein Functionality

Protein can be found inside the system of almost every plant and animal. Protein is also

crucial to the survival of all living terrestrial organisms including humans (Antonio et al. 2016).

Protein in foods are responsible for gelation, enzymatic reactions, bioactivity, and are the source

of most allergens in foods (Foegeding & Davis, 2011). Proteins come in all shapes and sizes. A

proteins shape is crucial to its function. If a protein in the form of an enzyme is to catalyze a

specific reaction, it needs to fit into the cell its effecting like a key. The order and type of amino

acids is what determines the shape of a protein, extended chains of amino acids can have infinite

combinations and have completely different behaviors (Monirujjaman & Ferdouse, 2014).

In the science lab, we looked at the functions of protein foams, these included: Versawhip

foam, gelatin foam, and egg protein foam. Starting with an egg foam dials into the denaturation

of a proteins teritiary structure into a more linear secondary or primary structure. The form of

denaturation in this egg foam system was pure shear force in the form of a kitchen aid mixer with

a whip attachment. Through excessive whipping of pure liquid egg whites, the protein found

within; ovalbumin, ovotransferrin, ovomucoid, and lysozyme (chemistryviews.org); begin to lose

native tertiary structures di-sulphur bridges breaking from its self and begin to form di-sulphur

bonds with other proteins at opposite moieties. This causes a network of proteins that entrap air

between lamellae and stack causing foam formation. Add a little sugar to this foam and you have

a meringue! Proteins functionality in meringue can next be torched with a little heat to cause a

maillard reaction which is a combination of reducing amino acids and reducing sugars (I know

its very complicated... dont crucify me) this reaction gives browning and toasty flavours

(Baking and Pastry, 2011). There were three types of meringues that were made in this lab, one at
a low pH, one neutral, and one alkaline. The low pH and alkaline were very unstable as the

excess pH levels caused extra denaturation of the proteins ending in synerisis. The ideal egg

white foam functions at a neutral pH that avoids extra denaturation of egg white proteins.

A following experiment deal with a gelatin protein foam, but unlike the egg white foam

which was made from a tepid system, the gelatin foam had heat energy added to it. When the

gelatin was heated, the proteins intra molecular bonds within became overwhelmed by the heated

environment and began to denature, although gelatins proteins somewhat reform through triple

helical junction points (Imeson, 2010), once heat has denatured and cooling begins to set in

hydrophobic areas of proteins that were exposed from heat begin to relink though di-sulphur

bonds and while doing so, trap water in the matrix causing a foam. This foam was used to make a

marshmallow, I added a little flavor to the matrix to mimic a peach cobbler type flavor of

marshmallow! This yielded not the best foam, while it indeed did classify as a foam because

there was a system of a gas dispersed in a liquid, the amount of aeration was minuscule

compared to those of the versawhipe and egg white foams. Although miniscule aeration

occurred, the foam was indeed permanent as for it was left for 24 hours to let the gelatin set;

solidifying the foam for an eternity!

Lastly was a foam made from versawhip, which is a blended powder consisting of a proprietary

modified soy protein (molecularrecipies.com, 2015). This powder was mixed with a apple cider

aqueas solution that was supplemented with a touch of xanthan gum to create an elastic synergy

that allowed for extra stability of the foam (Myhrvold, 2011). This structure held without major
synerisis or degradation for over two hours! While this structure stability is impressive, the taste

and aroma of dog vomit that the versawhip off put was a deal breaker.

Antonio, J., Ellerbroek, A., Silver, T., Vargas, L., & Peacock, C. (2016). The effects of a high
protein diet on indices of health and body composition a crossover trial in
resistance- trained men. Journal of the International Society of Sports
Nutrition,13(1). doi:10.1186/s12970-016-0114-2

Baking and Pastry Mastering the Art and Craft Art of the Chocolatier and Pastry Chef's
Companion Set. (2011). John Wiley & Sons Inc.

Cherry, J. P. (1981). Protein functionality in foods: based on a symposium at the 179th

Meeting of the American chemical Society; Houston - Tex., March 24-28, 1980.
Washington, D.C: American Chemical Society.

Imeson, A. (2010). Food Stabilisers, Thickeners and Gelling Agents. Chichester: Blackwell
Publishing.

Proteins Present in Egg White - Part of the Boiled Eggs Article. (n.d.). Retrieved April 05,
2017, from http://www.chemistryviews.org/details/ezine/1492619/.html

Foegeding, E. A., & Davis, J. P. (2011). Food protein functionality: A comprehensive

approach. Food Hydrocolloids,25(8), 1853-1864. doi:10.1016/j.foodhyd.2011.05.008

Monirujjaman, M., & Ferdouse, A. (2014). Metabolic and Physiological Roles of Branched-
Chain Amino Acids. Advances in Molecular Biology,2014, 1-6. doi:10.1155/2014/364976

Myhrvold, N., Young, C., Bilet, M., & Smith, R. M. (2011). Modernist cuisine: the art and
science of cooking. Bellevue, Wash. (3150 139th Ave. SE, Bellevue, WA 98005):
Cooking Lab.

Singh, H. (n.d.). Protein functionality and aggregation. Milk protein functionality in food
colloids. Special Publications Food Colloids,177-193. doi:10.1039/9781847552389-
00177
Versawhip. (2015, August 20). Retrieved April 05, 2017, from
http://www.molecularrecipes.com/hydrocolloid-guide/versawhip/