Trypsin

CAS No:	9002-07-07
EINECS No:	232-650-8
EC No:	3.4.21.4
Synonyms:	Bovine pancreas trypsin, porcine pancreas trypsin, pancreatic protease, pancreatic trypsin, parenzyme, serine protease trypsin, trypsin 1, trypsin serine endopeptidase, trypsinase, trypsinum, trypase

Product Summary

Trypsin is a serine protease enzyme commonly derived from porcine or bovine pancreas. It plays a vital role in protein digestion by cleaving peptide bonds at the carboxyl side of lysine and arginine residues. In biotechnology and biochemistry, trypsin is widely used for protein and cell research due to its highly specific cleavage pattern and compatibility with physiological conditions. Trypsinogen is the inactive precursor of trypsin.

Biochemical Function & Mechanism of Action

Trypsin belongs to the serine protease family. It hydrolyzes peptide bonds, specifically after the amino acids lysine or arginine. Trypsin uses a catalytic triad (serine, histidine, and aspartate) to perform nucleophilic attack on peptide bonds. The substrate fits into the S1 pocket of the enzyme, which has high specificity for basic residues.

Optimal conditions: pH 7.5-8.5, temperature 37°C.
Inhibitors: soybean trypsin inhibitor, TLCK, PMSF.

Applications in Scientific Research

Cell Biology: Detachment of adherent cells during passaging (e.g., in tissue culture).
Proteomic and mass spectrometry (MS): Used in bottom-up proteomics to breakdown proteins for MS analysis; Trypsin/Lys-C mixed enzymes enhance peptide identification in proteomic studies.
Molecular Biology: Isolation and purification of recombinant proteins.

Packaging & Storage

Source: porcine or bovine pancreas
Not less than 2500 USP trypsin units/mg, trypsin 1:250 and trypsin 30 FIP units/mg are available
Available as lyophilized powder.
Store in an airtight container at a temperature of 2 to 8°C, protected from light.

References

Deng Y, et al. 2022: Comparison of protein hydrolysis catalyzed by bovine, porcine, and human trypsins, J Agric Food Chem. 66(16):4219–32.
Szmola R, et al. 2003: Human mesotrypsin is a unique digestive protease specialized for the degradation of trypsin inhibitors, J Biol Chem. 278(49):48580-9.
Szmola R, Sahin-Tóth M. 2007: Chymotrypsin C (caldecrin) promotes degradation of human cationic trypsin: identity with Rinderknecht's enzyme Y, Proc Natl Acad Sci U S A. 104(27):11227-32.
Ma W, et al. 2005: Specificity of trypsin and chymotrypsin: loop motion controlled dynamic correlation as a determinant, Biophys J. 89(2):1183–93.
Gui F, et al. 2020: Trypsin activity governs increased susceptibility to pancreatitis in mice expressing human PRSS1R122H, J Clin Invest. 130(1):189-202.
Lerch MM, et al. 2000: The role of cysteine proteases in intracellular pancreatic serine protease activation, Adv Exp Med Biol. 477:403-11.
Vandermarliere E, et al. 2013: Getting intimate with trypsin, the leading protease in proteomics, Mass Spectrom Rev. 32(6):453-65.
Peräkylä M, Kollman PA. 2000: Why does trypsin cleave BPTI so slowly?, J Am Chem Soc. 122(14):3436–44.
Buchholz I. et al. 2020: The impact of physiological stress conditions on protein structure and trypsin inhibition of serine protease inhibitor Kazal type 1 (SPINK1) and its N34S variant, Biochim Biophys Acta Proteins Proteom. 1868(1):140281.
Huber R, Bode W. 1978: Structural basis of the activation and action of trypsin, Acc Chem Res. 11(3):114–122.
Šlechtová T, et al. 2015: Insight into trypsin miscleavage: Comparison of kinetic Constants of problematic peptide sequences, Anal Chem. 87(15):7636–43.
Xia Y-L, et al. 2020: The energetic origin of different catalytic activities in temperature-adapted trypsins, ACS Omega. 5(39):25077-86.