Rc USP Trypsin
Trypsin, a single chain protein of 223 amino acids, is a member of the Serine protease S1 family. It is 223 amino acids long — expressed in Pichia Pastoris — and is produced by the removal of N-terminal hexapeptide from Trypsinogen. The native form of Trypsin is termed as β –Trypsin and α-Trypsin results from the hydrolysis of it. The protease cleaves peptides at Lysine and Arginine residues on the C-terminal end, with an optimal activity at pH 7-9. USP grade Trypsin has a defined α:β ratio.
- Insulin and vaccine manufacturing
- Cell culture applications
- Food industry
- Cosmetic industry
- 100% AOF
- Zero risk of contamination by adventitious agents
- High purity; free of contaminating proteases such as Amylase, Chymotrypsin and Carboxypeptidases
- Description: Clear, colorless to pale greenish brown, odorless liquid
- pH: 2.0-3.0
- Protein content by UV 280: >60 mg/ml
- Specific activity: >3800 USP units/mg of protein
- Purity by RP HPLC:
- ≥ 70% for the peak area of β-Trypsin
- ≤ 20% for the peak area of α-Trypsin
- Microbial limit tests:
- TVAC: <100 cfu/ml
- TYMC: <10 cfu/ml
- Pathogens:
- E. Coli: Shall be absent
- Salmonella sp: Shall be absent
- Pseudomonas aeruginosa: Shall be absent
- Staphylococcus aureus: Shall be absent
- Description: White to off white odourless powder
- Solubility: An amount equivalent to 500,000 USP Trypsin units is soluble in 10ml of water and 10ml of saline TS
- Enzyme activity by USP method: >2500 USP units/mg of powder
- Protein content by UV 280 : ≥ 0.60 mg/mg of powder
- Specific activity: >3800 USP units/mg of protein
- Purity by RP HPLC:
- ≥70% for the peak area of β-Trypsin
- ≤ 20% for the peak area of α-Trypsin
- Loss of Drying: NMT 5.0%
- Residue on ignition: NMT 2.5%
- Microbial limit tests:
- TVAC: <10,000 cfu/gm
- TYMC: <100 cfu/ml
- Pathogens:
- E. Coli: Shall be absent
- Salmonella sp: Shall be absent
- Pseudomonas aeruginosa: Shall be absent
- Staphylococcus aureus: Shall be absent
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CIN: U02423KA2005PTC036770
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