Natural protein consists of complex, folded and coiled individual molecules. Loose bonds across the folds and coils hold each protein molecule in a tight, separate unit. These bonds can be disrupted when exposed to heat or acid, or by physical means such as whipping, causing the protein to denature. When two unfolded protein molecules with their oppositely charged ends approach each other, the molecules unite. Essentially, millions of protein molecules join in a three-dimensional network, or simply, they coagulate, causing the egg product to change from a liquid to a semi-solid or solid. Coagulation influences egg products’ ability to foam, seal, thicken and more. There are more than 40 different proteins in a whole egg, some only located in the white and others predominantly in the yolk. These proteins influence the rate of denaturation and coagulation. Egg white protein coagulates between 144° F and 149° F (62.2° C and 65° C); egg yolk protein coagulates between 149° F and 158° F (65° C and 70° C); and whole egg protein coagulates between 144° F and 158° F (62.2° C and 70° C). However, a number of variables influence the rate of coagulation, as well as the ability of the proteins to remain in the three-dimensional network.
Watch this video to learn more about egg products and coagulation in baked desserts.
Watch this video about egg products and coagulation in refrigerated desserts.
Functional Properties & Uses