Trypsin
Trypsin Manufacturer | Proteolytic Enzyme API Headline: High Activity Trypsin Manufacturer | Specific Proteolytic Enzyme (CAS: 9002-07-7) Sub-headline: 1:250 / 2500 USP Units | High Specificity Serine Protease | Porcine/Bovine Origin Unique Selling Proposition (USP): • Targeted Cleavage: Specifically cleaves peptide bonds at the carboxyl side of lysine and arginine, essential for precise protein hydrolysis. • High Purity Options: Available in crystallized forms for pharmaceutical applications and standard powders for food/industrial use. • Viral Safety: Rigorously screened and processed to ensure freedom from viral contaminants (e.g., PPV).
Introduction
Trypsin (CAS: 9002-07-7) is a serine protease enzyme found in the digestive system of many vertebrates, where it hydrolyzes proteins. It is produced in the pancreas as the inactive proenzyme trypsinogen.
Our Trypsin is extracted and purified typically from porcine (pig) or bovine (cow) pancreas. It is widely used in biotechnology (cell dissociation), food processing (protein hydrolysates), and pharmaceuticals (wound cleaning, digestive aids). Its specificity makes it an indispensable tool in proteomics for protein sequencing.
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trypsin
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Functions
1.Cell Culture Dissociation
• Mechanism: Hydrolyzes extracellular matrix proteins.
• Action: Detaches adherent cells from culture vessels and dissociates tissue into single-cell suspensions without damaging the cell membrane (when used correctly).
2.Protein Hydrolysis
• Mechanism: Cleaves peptide bonds specifically after basic amino acids (Lysine, Arginine).
• Action: Used to produce hypoallergenic infant formulas (by breaking down allergenic proteins) and bioactive peptides.
3.Wound Debridement
• Mechanism: Proteolytic digestion of necrotic tissue.
• Action: Helps remove dead tissue from wounds (often in combination with Chymotrypsin), promoting faster healing and reducing infection risk.
Applications
1.Biopharma & Research
• Application: Trypsin-EDTA solutions for cell culture passaging.
• Why it works: The combination with EDTA (which chelates calcium) enhances the efficiency of cell detachment.
2.Food Industry
• Application: Bakery (dough conditioning) and Infant Formula.
• Why it works: Improves dough extensibility by modifying gluten network; reduces allergenicity of milk proteins.
3.Pharmaceuticals
• Application: Enteric-coated tablets for inflammation and edema (often with Bromelain/Rutoside).
• Why it works: Systemic enzyme therapy uses trypsin to modulate the immune response and reduce swelling.
Flow Chart
1.Sourcing: Frozen pancreas glands (Porcine/Bovine) from inspected sources.
2.Mincing & Extraction: Acid extraction to solubilize zymogens.
3.Activation: Controlled pH adjustment and addition of calcium to auto-activate Trypsinogen to Trypsin.
4.Clarification: Filtration to remove tissue debris.
5.Purification: Salt fractionation (Ammonium Sulfate) or Affinity Chromatography.
6.Crystallization: Formation of high-purity crystals (for pharma grade).
7.Drying: Lyophilization (Freeze Drying).
8.Milling & Blending: Standardization to specific activity (e.g., 1:250).
9.Packaging: 1kg/5kg Aluminum Tins (Moisture sensitive).
Quality Standard of Lactoferrin
Product: Trypsin 1:250 / 2500 USP
CAS: 9002-07-7
| Item | Specification | Result |
| Appearance | White to off-white crystalline powder | Conforms |
| Activity (USP) | ≥ 2500 Units/mg | 2650 Units/mg |
| Activity (1:250) | Digests 250x weight of casein | Conforms |
| Chymotrypsin | < 5% (Specific Limit) | 2.5% |
| Loss on Drying | ≤ 5.0% | 3.1% |
| Residue on Ignition | ≤ 2.5% | 1.0% |
| pH (1% solution) | 3.0 - 5.0 | 4.1 |
| Microbial Limit | TAMC < 1000 CFU/g | Conforms |
Method of Analysis of Lactoferrin
Test Method: USP / BAEE Assay
• Procedure: Spectrophotometric measurement of the rate of hydrolysis of a synthetic substrate, usually BAEE (N-Benzoyl-L-arginine ethyl ester), at 253 nm.
• Differentiation: Specific inhibitors (like TLCK) can be used to distinguish Trypsin activity from Chymotrypsin contamination.
Reference Chromatogram of Lactoferrin Reference Substance
(Note: Purity is often assessed by electrophoresis)
SDS-PAGE should show a primary band at approximately 23.8 kDa. High purity grades (Crystallized) will show minimal bands for other pancreatic enzymes.
Stability and Safety
Stability Studies
• Autolysis: Trypsin undergoes autolysis (self-digestion) in solution, especially at neutral/alkaline pH.
• Stability: Stable in dry form. In solution, it is most stable at very acidic pH (pH 3).
• Shelf Life: 24 Months when stored at 2-8°C. Room temperature storage significantly reduces activity over time.
Safety & Handling (MSDS Summary)
• Classification: Respiratory Sensitizer / Skin Irritant.
• Handling: Strict dust control. Inhalation can cause severe allergic reactions (asthma). Avoid skin contact (can digest skin proteins).
• Storage: Refrigerate (2-8°C). Keep tightly sealed.
Customer Comments
Lab Manager, BioTech Research (USA)
2026.02.24
★★★★☆
R&D Director, Functional Proteins Ltd (Netherlands)
2026.02.24
★★★★☆
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FAQ
What is the difference between Trypsin 1:250 and pure USP Trypsin?
1:250 is a crude grade where 1 part enzyme digests 250 parts casein (common in tissue culture). USP Trypsin is a purified, crystallized grade measured in USP Units (typically >2500 Units/mg), used for pharma and high-precision applications.
How do I stop the enzyme reaction?
Trypsin activity can be inhibited by adding serum (which contains alpha-1 antitrypsin), soybean trypsin inhibitor, or by lowering the pH below 3.
Is it virus-free?
Our pharma-grade Trypsin undergoes viral inactivation steps (e.g., gamma irradiation or pH treatment) to ensure safety, especially from porcine parvovirus (PPV).
References
1.Olsen, J.V., et al. (2004). "Trypsin cleaves exclusively C-terminal to arginine and lysine." Molecular & Cellular Proteomics.
2.United States Pharmacopeia (USP) Monograph: Crystallized Trypsin.
3.Freshney, R.I. (2010). "Culture of Animal Cells: A Manual of Basic Technique and Specialized Applications." (Reference for cell dissociation).
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