AP BIOLOGY

Detailed explanation-1: -Trypsin cleaves the peptide bond between the carboxyl group of arginine or the carboxyl group of lysine and the amino group of the adjacent amino acid. The rate of cleavage occurs more slowly when the lysine and arginine residues are adjacent to acidic amino acids in the sequence or cystine.

Detailed explanation-2: -Trypsin breaks down the proteins into smaller peptides by hydrolysis reaction. It secretes as an inactive form of trypsinogen, which further gets active to act.

Detailed explanation-3: -Trypsin breaks down protein into peptides through a hydrolysis reaction. Hydrolysis occurs when a bond is broken in the presence of water. There are three main amino acids within trypsin’s active site: serine, histidine, and aspartate.

Detailed explanation-4: -Specificity: Pepsin hydrolyzes peptide bonds between large hydrophobic amino acid residues, whereas trypsin hydrolyzes peptide bonds at the C-terminal side of lysine or arginine. Function: Pepsin acts on proteins and converts them into peptones, while trypsin converts peptones into polypeptides.

Detailed explanation-5: -Trypsin is an enzyme that aids with digestion. An enzyme is a protein that speeds up a certain biochemical reaction. Trypsin is found in the small intestine. It can also be made from fungus, plants, and bacteria.