Trypsin is an enzyme categorized as a pancreatic serine protease that is found in the digestive system of many vertebrates; it helps by hydrolyzing proteins. The trypsin enzyme breaks peptide chains mainly at the carboxyl side of the amino acid lysine or arginine. It can be obtained in white lyophilized or in a crystalline powder form.
Trypsin aids in the digestion of protein in the small intestine. It breaks down the proteins, escalating the process that began in the stomach. It can also be termed as a proteolytic enzyme or proteinase.
Trypsin preparations are widely used in food processing and also as a baking enzyme as it improves the workability of dough, in the extraction of seasonings and flavorings from vegetable or animal proteins, and in the manufacture of sauces, also used to control the aroma formation in cheese and milk products.
It is also used to improve the texture of fish products, somewhat like a meat tenderizer, in the cold stabilization of beer, in the production of hypoallergenic food where proteases break down specifically targetted allergenic proteins into nonallergenic peptides. This enzyme is also utilized in cell and tissue development as well as in the peptide sequencing techniques used for protein identification. Trypsin is immensely useful for dissolving blood clots, treating inflammation, and dissociating dissected cells before fixing and sorting the wound.