Digestion in duodenum:
The main enzymes of the pancreatic juice which acts on proteins are a) Trypsin, b) Chymotrypsin, c) Carboxy peptidase, d) Elastases and e) Collagenases Trypsin:
Trypsin, a proteinase is secreted in the inactive zymogen type known as trypsinogen. It is activated through enterokinase and as well autocatalytically in the existence of calcium.
It is an endopeptidase which is particular for peptide linkages created by carboxyl groups of basic amino acids, they are arginine, lysine. The hydrolytic products are proteoses, peptones, polypetides, di and tri peptides. It cannot hydrolyze a peptide linkage that includes proline.
Trypsin activates proelastase to elastase, chymotrypsinogen to chymotrypsin, fibrinogen to fibrin.
The optimum pH of it is 8 – 9.Chymotrypsin:
Chymotrypsin is an endopeptidase that is secreted in the inactive form like chymotrypsinogen. It is activated through trypsin and as well autocatalytically. It hydrolyses peptide linkages along with carboxyl group of aromatic amino acids such as tryptophan, tyrosine and phenyl alanine.
The optimum pH of it is 7 - 8
Carboxy peptidase:
Two kinds of carboxy peptidases, carboxy peptidase A and B are well known. Carboxy peptidase A is a metallo enzyme which consists of zinc. Both of them are exopeptidases. Carboxy peptidase A is particular for aromatic amino acids at the C terminal end, when carboxy peptidase B is particular for basic amino acids at the C terminal end.
The optimum pH for both lies between 7-8.
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