Final answer:
Enterokinase activates trypsinogen to trypsin, which in turn activates other pancreatic enzymes option (a) such as chymotrypsinogen to chymotrypsin, aiding in the proper digestion of proteins within the small intestine.
Step-by-step explanation:
The role of enterokinase and trypsin in the activation of pancreatic enzymes option (a) is vital for the digestion of proteins in the small intestine. Enterokinase, an enzyme located in the wall of the small intestine, activates trypsinogen to its active form, trypsin, by clipping off a specific peptide from its structure. Once active, trypsin then proceeds to activate other pancreatic proteases, such as chymotrypsinogen to chymotrypsin and procarboxypeptidase to carboxypeptidase. This cascade of activation is essential because it prevents the pancreatic enzymes from digesting the pancreas itself, which could lead to pancreatitis.
These activated enzymes, trypsin and chymotrypsin, catalyze the breakdown of proteins into smaller peptides through the process of proteolysis. These peptides are further broken down into amino acids by other enzymes, which are then absorbed into the bloodstream for use in protein synthesis throughout the body.