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Chymotrypsin is a serine protease enzyme synthesized in the pancreas and secreted as an inactive precursor (chymotrypsinogen), which is activated in the duodenum. It acts as a digestive enzyme by catalyzing the hydrolysis of peptide bonds in proteins and polypeptides—preferentially those with aromatic amino acids such as tryptophan, tyrosine or phenylalanine on the N-terminal side. In medicine and supplements it is used for its anti-inflammatory and anti-edematous properties to reduce swelling associated with trauma or surgery and to promote tissue repair. It has also been used during cataract surgery to reduce damage to ocular tissues[2][3][4][6]. The mechanism of action involves proteolytic cleavage of protein substrates via a catalytic triad (ser195-his57-asp102) at its active site[6].
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