chymotrypsina

Chymotrypsin is a digestive enzyme that functions as a protease. It is synthesized in the pancreas as an inactive proenzyme called chymotrypsinogen. This zymogen is then secreted into the small intestine, where it is activated by the enzyme trypsin. Once activated, chymotrypsin plays a crucial role in the breakdown of proteins into smaller peptides. It specifically cleaves peptide bonds on the carboxyl side of aromatic amino acid residues, such as tyrosine, phenylalanine, and tryptophan. This enzymatic activity is essential for nutrient absorption and allows the body to utilize the amino acids from dietary proteins. Chymotrypsin is also used therapeutically, for example, in the treatment of inflammatory conditions and in wound debridement. Its precise action on proteins makes it a valuable tool in both biological processes and medical applications. The optimal pH for chymotrypsin activity is alkaline, consistent with its function in the small intestine.