chymotrypsín

Chymotrypsin is a digestive enzyme that functions as a protease, meaning it breaks down proteins. It is synthesized in the pancreas as an inactive precursor called chymotrypsinogen and released into the small intestine. There, it is activated by the enzyme trypsin. Once activated, chymotrypsin hydrolyzes peptide bonds, primarily cleaving after aromatic amino acids such as tyrosine, tryptophan, and phenylalanine. This enzymatic activity is crucial for the digestion of dietary proteins, breaking them down into smaller peptides and amino acids that can be absorbed by the body.

Beyond its role in digestion, chymotrypsin has found various therapeutic applications. It is used in medicine to help reduce inflammation and swelling, particularly after surgery or in certain medical conditions. It is also utilized in wound healing to debride dead tissue. In research settings, chymotrypsin is a valuable tool for protein analysis and manipulation due to its specific cleavage patterns. Its precise action on protein substrates makes it an important enzyme in both biological processes and biotechnological applications.