BIOMOLECULES AND ENZYMES

Detailed explanation-1: -A protein becomes denatured when its normal shape gets deformed because some of the hydrogen bonds are broken. Weak hydrogen bonds break when too much heat is applied or when they are exposed to an acid (like citric acid from lemon juice).

Detailed explanation-2: -When a solution of a protein is boiled, the protein frequently becomes insoluble-i.e., it is denatured-and remains insoluble even when the solution is cooled. The denaturation of the proteins of egg white by heat-as when boiling an egg-is an example of irreversible denaturation.

Detailed explanation-3: -Heat can be used to disrupt hydrogen bonds and non-polar hydrophobic interactions. This occurs because heat increases the kinetic energy and causes the molecules to vibrate so rapidly and violently that the bonds are disrupted. The proteins in eggs denature and coagulate during cooking.

Detailed explanation-4: -During cooking, when the proteins are heated, the molecules become agitated and move around causing the intermolecular bonds between molecules to be broken. This allows the protein to denature (change shape) which changes the texture of foods.