Trypsin and Chymotrypsin

Trypsin and chymotrypsin are essential serine proteases synthesized as inactive zymogens, trypsinogen and chymotrypsinogen, in the exocrine pancreas and subsequently activated in the small intestine (UniProt, 2023). They play a fundamental role in the digestive system by hydrolyzing dietary proteins into smaller peptides; trypsin specifically cleaves at the carboxyl side of lysine or arginine residues, while chymotrypsin targets aromatic amino acids (StatPearls, 2023). Beyond their digestive utility, these enzymes are used therapeutically in combination to manage edema and inflammation associated with trauma or surgery by facilitating the resorption of fibrin deposits and necrotic tissue (PubMed, 2022). In certain pathological states, such as acute pancreatitis, the premature activation of these enzymes leads to tissue autodigestion, making them critical targets for protease inhibitors like camostat and aprotinin (PubChem, 2024). Their clinical relevance spans from enzyme replacement therapy in pancreatic insufficiency to serving as diagnostic markers for pancreatic health.

Other names

Serine endopeptidasesPancreatic proteasesTrypsin-Chymotrypsin combinationPRSS1 and CTRB1Chymotrypsinogen and Trypsinogen

As therapeutic agents, trypsin and chymotrypsin catalyze the hydrolysis of peptide bonds in proteins, which helps dissolve fibrin clots and necrotic debris, thereby reducing inflammation and promoting tissue repair (PubChem, 2024). When these enzymes are the targets of therapy, inhibitors bind to their active sites to prevent the proteolytic degradation of host tissues, which is particularly relevant in preventing autodigestion during acute pancreatitis (StatPearls, 2023).