Final answer:
Proteolytic enzymes in pancreatic secretions are essential for breaking down proteins in the small intestine. These enzymes are secreted in an inactive form and are activated in the small intestine by other enzymes such as enteropeptidase and trypsin. Bicarbonate also secreted by the pancreas helps to neutralize acid and facilitate enzyme activity.
Step-by-step explanation:
Pancreatic secretions contain proteolytic enzymes which are crucial for protein digestion in the small intestine. These enzymes, such as trypsinogen and chymotrypsinogen, are secreted in an inactive form to prevent damage to the pancreas. Once inside the small intestine, trypsinogen is converted to trypsin by the enzyme enteropeptidase, which is secreted by the intestinal mucosa. Trypsin then further activates other enzymes such as chymotrypsinogen to chymotrypsin, which catalyzes the hydrolysis of peptide bonds in proteins, impacting specifically the aromatic and basic amino acids. Additionally, procarboxypeptidase is activated to carboxypeptidase by trypsin, breaking the peptide bonds at the free carboxyl end of a protein chain, releasing free amino acids.
Bicarbonate-rich pancreatic juices also play an important role by neutralizing the acidic chyme and providing an optimal environment for the enzymatic activity.