Statements of Trypsin

Trypsin which can be found in the digestive system of many vertebrates, where it hydrolyses proteins is a serine protease. It is produced in the pancreas as the inactive proenzyme trypsinogen. It cleaves peptide chains mainly at the carboxyl side of the amino acids lysine or arginine, except when either is followed by proline. It is used for numerous biotechnological processes. The process is commonly referred to as trypsin proteolysis or trypsinisation, and proteins that have been digested/treated with trypsin are said to have been trypsinized.

The role of trypsin in duodenal trypsin hydrolysis of amino acid polypeptide. This is a necessary step, because the absorption of protein peptide (small protein) is too large and can not be absorbed through the small intestine wall. Trypsin catalyzes the hydrolysis of peptide bonds. Invalid zymogen ttrypsin of the original form of the production of trypsin in the pancreas. When the pancreas to stimulate cholecystokinin secretion, and then to the first part of the small intestine (duodenum) through the pancreatic duct. Once in the small intestine, the enzyme enteropeptidase activated protein cleaved into trypsin. It can activate normal additional trypsin (autocatalytic), so only a small amount of enteropeptidase is necessary to start the reaction. This activation mechanism is common for most serine proteases, helps to prevent pancreas autodegradation.

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