Trypsin is a pancreatic serine protease found in many vertebrates’ digestive systems, where it hydrolyses proteins.
Trypsin cleaves peptide chains mainly at the carboxyl side of the amino acids lysine or arginine. Its appearance is a white lyophilized or crystalline powder.
The enzyme could easily be autolyzed and is soluble in water but insoluble in ethanol, ether, and glycerol.
Trypsin enzyme can be employed in ointment or as a wet or dry dressing. In solution, trypsin may be used as an aerosol to liquefy tenacious sputum in bronchial disorder.
Trypsin preparations are widely used in food processing as a baking enzyme to improve dough workability, extract seasonings and flavorings from vegetable or animal proteins, and manufacture sauces, to control aroma formation in cheese and milk products.
It is also used to improve the texture of fish products, as a meat tenderizer, in cold stabilization of beer, and in the production of hypoallergenic food where proteases break down specific allergenic proteins into nonallergenic peptides.