HUMAN NUTRITION

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: -Pepsin is a stomach enzyme that serves to digest proteins found in ingested food. Gastric chief cells secrete pepsin as an inactive zymogen called pepsinogen. Parietal cells within the stomach lining secrete hydrochloric acid that lowers the pH of the stomach. A low pH (1.5 to 2) activates pepsin.

Detailed explanation-4: -Trypsin is most effective on partially digested proteins. It also digests some proteins, such as protamines and histones, that cannot be digested by pepsin. The products of trypsin digestion are amino acids and various polypeptides.

Detailed explanation-5: -So, the correct answer is ‘true’.