Trypsin

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

Where is Trypsin used?

• Food processing: production of protein hydrolysates and peptide fractions from soy, whey, and meat proteins
• Pharmaceutical: enzyme preparations and topical debridement products targeting necrotic tissue
• Biotech: standard reagent for detaching adherent mammalian cells
• Proteomics and peptide mapping: primary digestion tool before mass spectrometry analysis
• It cleaves peptide bonds at specific lysine and arginine residues for controlled protein hydrolysis.
• In cell detachment, EDTA is added to trypsin solution as a chelating agent to bind calcium and magnesium, weakening cell-cell adhesion and improving trypsin's access to target peptide bonds.
• In the biopharmaceutical field, the main application was insulin production, and it was soon used in other cell culture fields.

Good to know: Activity is expressed in USP, BAEE, or TAME units depending on the application. Cell culture applications typically require sequencing-grade or recombinant forms to minimize variability.

Formulation notes

• Activity is strongest at pH 7-9 and 37 °C.
• Activity is inhibited by serine protease inhibitors such as PMSF and TLCK, and by metal ion chelators such as EDTA.
• Non-recombinant trypsin has a chymotrypsin limit of at most 50 units per 2500 units of trypsin, while recombinant trypsin has no contamination with mirosinase and other impure enzymes.
• The specific activity of non-recombinant trypsin is ≥2500 USP units/mg protein, while that of recombinant trypsin is ≥3800 USP units/mg protein.

Typical specification

• The specificity of purified trypsin is improved by TPCK treatment, which inactivates chymotrypsin.
• Porcine Trypsin 1:250 is available in a gamma-irradiated form.
• For oral use, it must be protected from gastric destruction, so enteric-coated or delayed-release forms are required.

Regulatory status

• Trypsin has ATC codes B06AA07, D03BA01 and M09AB52.
• Recombinant trypsin is expressed using recombinant E. coli or yeast systems and is free from exogenous viral contamination.

Storage, packaging and handling

• Trypsin should be stored at -15 to -20 °C.

Frequently asked questions about Trypsin

In which applications is recombinant trypsin used?

Recombinant trypsin is used in immune cell therapy.

Technical content is compiled and updated by the SoleChem product team from public technical sources; the certificate of analysis (COA) governs product-specific specifications.