Trypsin

Trypsin (CAS 9002-07-7) is a serine protease enzyme sourced primarily from bovine or porcine pancreas, also marketed under trade names such as Parenzyme, Tryptar, and Trypure.

It cleaves peptide bonds at specific lysine and arginine residues, making it a standard tool for controlled protein hydrolysis across food, pharmaceutical, and biotech manufacturing.

In food processing, it is used to produce protein hydrolysates and peptide fractions from soy, whey, and meat proteins. This enables manufacturers to improve digestibility and reduce allergenicity.

Pharmaceutical formulators use it in enzyme preparations and topical debridement products targeting necrotic tissue. In biotech workflows, it is the standard reagent for detaching adherent mammalian cells.

Proteomics and peptide mapping workflows also rely on this enzyme as the primary digestion tool before mass spectrometry analysis. It is supplied as a lyophilized powder or solution.

Activity is expressed in USP, BAEE, or TAME units depending on the application. Established grades include Ph. Eur. and research-grade specifications for various industrial uses.

Purity levels range from crude pancreatin fractions to highly purified single-enzyme preparations. Cell culture applications typically require sequencing-grade or recombinant forms to minimize variability.