Q.Describe the digestive role of chymotrypsin. Which two other digestive enzymes of the same category are secreted by its source gland?

Chymotrypsin is a proteolytic (protein-digesting) enzyme secreted by the pancreas in its inactive form, chymotrypsinogen, which is activated in the duodenum by trypsin. Once active, chymotrypsin functions as an endopeptidase: it cleaves internal peptide bonds within proteins, proteoses and peptones, breaking them down into smaller peptides. It also has the distinctive additional action of coagulating (clotting) the milk protein casein, similar to rennin's action in the stomach.

Chymotrypsin belongs to the same category of pancreatic proteolytic enzymes as two others:

• Trypsin (from trypsinogen, activated by enterokinase) — also an endopeptidase, breaking proteins/peptones into peptides, and it is itself responsible for activating chymotrypsinogen.
• Carboxypeptidase (from procarboxypeptidase, activated by trypsin) — an exopeptidase that removes amino acids one at a time from the carboxyl end of peptide chains. …

State chymotrypsin's activation pathway (chymotrypsinogen → chymotrypsin via trypsin), its two actions (peptide-bond cleavage and milk clotting), then name the other p …

• Forgetting chymotrypsin's milk-clotting action in addition to its general proteolytic role. …