Trypsin consists of a single chain polypeptide of 223 amino acid residues. It is a member of the serine protease family. It composed of two subunits, α-trypsin and β-trypsin. α-Trypsin is composed of two peptide chains and β-trypsin is composed of one chain.

• Soluble in water
• Extinction coefficient (E1%): E1%280 = 14,3 (Lit.)
• Isoelectric point (pI): 10,5
• Enzyme commission number: E.C. 3.4.21.4
• Typical working concentration for the removal of adherent cells from a culture surface: 2,5% w/v solution
• Optimum pH: Approximately 8,0 (Lit.)

Trypsin can be used to dissolve blood clots in its microbial form and treat inflammation in its pancreatic form. Trypsin is commonly used in biological research.

Inhibitors: Trypsin is inhibited by organophosphorus compounds such as diisopropyl fluorophosphate and natural trypsin inhibitors from pancreas, soybean, lima bean and egg white. Silver ions are also potent inhibitors. Specific inhibitors are AEBSF, antipain, aprotinin, DFP, leupeptin, PMSF, TLCK, and Trypsin Inhibitor. Specificity: The protease activity of trypsin is highly specific toward positively charged side chains with lysine and arginine. Forms complexes with a2-macroglobulin. Can be used in the isolation of intact, detergent-free phycobilisomes and in the hydrolysis/condensation of carboxylic ester bonds.

Unit definition: One unit hydrolyses one µmole of TAME per minute at 25 °C, pH 8,2, in the presence of ionised calcium.