Trypsin Chymotrypsin ""''

Trypsin Chymotrypsin
STERICHYME FORTE  
Trypsin and chymotrypsin are both enzymes that play crucial roles in protein digestion. They are produced and released by the pancreas into the small intestine, where they help break down dietary proteins into smaller peptides and amino acids, which can then be absorbed by the body.
Trypsin is a serine protease enzyme that specifically cleaves peptide bonds on the carboxyl side of the basic amino acids lysine and arginine. It is released as an inactive precursor called trypsinogen, which is activated by another enzyme called enteropeptidase (also known as enterokinase) in the small intestine. Once activated, trypsin helps to further digest the partially broken-down proteins into smaller peptides.
Chymotrypsin is another serine protease enzyme that cleaves peptide bonds on the carboxyl side of aromatic amino acids, which include phenylalanine, tyrosine, and tryptophan. Like trypsin, chymotrypsin is also released as an inactive precursor, chymotrypsinogen, which is activated by trypsin. Once activated, chymotrypsin contributes to the degradation of peptides into even smaller fragments.
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