trypsin

Examples of trypsin in the following topics:

• Chemical Digestion of Carbohydrates, Proteins, Lipids, and Nucleic Acids

  • Protein digestion occurs in the stomach and the duodenum through the action of three primary enzymes: pepsin, secreted by the stomach, and trypsin and chymotrypsin, secreted by the pancreas.
  • Thus, trypsin is secreted by the pancreas in the form of trypsinogen, which is activated in the duodenum by enterokinase to form trypsin.
  • Trypsin then cleaves proteins to smaller polypeptides.

• Associated Organs

  • These zymogens are inactivated forms of trypsin and chymotrypsin.
  • Once released in the intestine, the enzyme enterokinase, which is produced by the intestinal mucosa, activates trypsinogen by cleaving it to form trypsin.
  • The free trypsin then cleaves the rest of the trypsinogen and chymotrypsinogen to their active forms.

• Digestive Processes of the Small Intestine

  • Proteolytic enzymes, including trypsin and chymotrypsin, secreted by the pancreas, cleave proteins into smaller peptides.

• Mechanisms of Chemical Digestion

  • The proteolytic enzymes are all secreted in an inactive form, to prevent auto-digestion, and are activated in the lumen of the gut: by HCl in the case of the stomach pepsinogen; by enteropeptidase and trypsin in the case of the pancreatic enzymes.

• Digestive Properties of the Stomach

  • The biological effects of salivary EGF include healing of oral and gastroesophageal ulcers, inhibition of gastric acid secretion, and stimulation of DNA synthesis as well as mucosal protection from intraluminal injurious factors such as gastric acid, bile acids, pepsin, and trypsin, and to physical, chemical, and bacterial agents.

• Absorption of Monosaccharides, Amino Acids, Dipeptides, Tripeptides, Lipids, Electrolytes, Vitamins, and Water

  • Proteolytic enzymes, including trypsin and chymotrypsin, are secreted by the pancreas and cleave proteins into smaller peptides.