where is trypsin found in the digestive system
Trypsin Trypsin is produced as the inactive zymogen trypsinogen in the pancreas. When the pancreas is stimulated by cholecystokinin, it is then secreted into the first part of the small intestine (the duodenum) via the pancreatic duct. Once in the small intestine, the enzyme enteropeptidase activates trypsinogen into trypsin by proteolytic cleavage. Autocatalysis does not happen with trypsin, as trypsinogen is a poor substrate, therefore enzymatic damage to the pancreas is avoided.[6]
Trypsin Trypsin (EC 3.4.21.4) is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyzes proteins.[2][3] Trypsin is formed in the small intestine when its proenzyme form, the trypsinogen produced by the pancreas, is activated. Trypsin cleaves peptide chains mainly at the carboxyl side of the amino acids lysine or arginine, except when either is followed by proline.[4] 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.[5] Trypsin was discovered in 1876 by Wilhelm Kühne.[6]
Jejunum The jejunum (/dʒɪˈdʒuːnəm/[2][3]) is the second part of the small intestine in humans and most higher vertebrates, including mammals, reptiles, and birds.
Protein (nutrient) Most proteins are decomposed to single amino acids by digestion in the gastro-intestinal tract.[14]