kimotripsinës

Kimotripsinës is a serine protease that plays a significant role in protein digestion. It is synthesized in the pancreas as an inactive precursor called chymotrypsinogen. Upon entering the small intestine, chymotrypsinogen is activated by the enzyme trypsin, which cleaves it to form active chymotrypsin.

Chymotrypsin is a key enzyme in the digestive system, primarily responsible for breaking down proteins into smaller peptides. It exhibits specificity for peptide bonds where the preceding amino acid residue is aromatic, such as phenylalanine, tyrosine, and tryptophan. This targeted action helps to further digest dietary proteins into amino acids, which can then be absorbed by the body.

Beyond its digestive function, chymotrypsin is also involved in other physiological processes. It has been studied for its potential therapeutic applications, particularly in wound healing and the breakdown of necrotic tissue. Research has also explored its role in inflammation and immune responses. The enzyme's structure features an active site with a catalytic triad of amino acids: aspartate, histidine, and serine, which are crucial for its enzymatic activity. Its optimal functioning occurs in the alkaline environment of the small intestine.