BIOMOLECULES AND ENZYMES

Detailed explanation-1: -The denaturation of the proteins of egg white by heat-as when boiling an egg-is an example of irreversible denaturation. The denatured protein has the same primary structure as the original, or native, protein.

Detailed explanation-2: -Whenever eggs are cooked with heat, the egg whites turn from clear to white, and the gel becomes more rubbery. As heat denatured the proteins in the egg white, it broke apart some of the bonds (mostly hydrogen bonds) that were holding the proteins in their original shape.

Detailed explanation-3: -Cooking an egg (or many other protein-rich foods) largely involves denaturing the proteins, and cross-linking them with each other to form the rubbery, white substance we are familiar with eating.

Detailed explanation-4: -Common examples When food is cooked, some of its proteins become denatured. This is why boiled eggs become hard and cooked meat becomes firm. A classic example of denaturing in proteins comes from egg whites, which are largely egg albumins in water.

Detailed explanation-5: -Denaturation ("changing the nature") happens when protein molecules unravel from their naturally coiled state. With eggs, this happens most frequently when they’re heated or beaten, but denaturation can also be prompted by salt, acids (such as vinegar), alkalies (such as baking soda), and freezing.