Trypsin
Enzyme Preparations
9002-07-7
(C₄H₅NO₃)n
$7.07 ~ $10.61
Food
Free sample from 100g(NF)
One unit of:25kg/barrel
One unit of:25kg/barrel
25kg/barrel
Product Info
What is Trypsin?
Trypsin is a protease enzyme derived from animal sources used as a processing aid to hydrolyze proteins for uses such as clarifying beverages and producing protein hydrolysates.
How is Trypsin made?
| Step No. | Production Stage | Key Action | Control Point & Note |
|---|---|---|---|
| 1 | Raw Material Sourcing | Collect fresh porcine or bovine pancreases from approved, inspected abattoirs. | Control Point: Glands must be harvested immediately post-mortem and rapidly frozen (e.g., below -20°C) to prevent enzyme degradation (autolysis). Note: Full traceability of the animal source is critical for quality and safety. |
| 2 | Extraction | Homogenize the minced pancreas tissue in a chilled, acidic buffer (e.g., sulfuric acid at pH 2.5-3.0) to extract the inactive precursor, trypsinogen. | Control Point: Maintain temperature between 0-4°C and a low pH. Note: The acidic environment prevents premature activation of trypsinogen and inhibits microbial growth. |
| 3 | Activation | Adjust the pH of the extract to approximately 7-9 and add a small amount of active trypsin to initiate the conversion of trypsinogen to active trypsin. | Control Point: Monitor and control pH, temperature (e.g., 25°C), and reaction time. Enzyme activity is assayed to determine the endpoint. Note: This is an autocatalytic process where newly formed trypsin activates more trypsinogen. |
| 4 | Clarification | Remove insoluble tissue debris, fats, and precipitated proteins from the activated solution using centrifugation and filtration. | Control Point: Ensure the resulting supernatant is clear to avoid fouling downstream equipment. Note: Filter aids like diatomaceous earth may be used to improve clarity. |
| 5 | Purification | Isolate and purify the trypsin using methods like fractional precipitation (e.g., with ammonium sulfate) and/or chromatography (e.g., ion-exchange or affinity chromatography). | Control Point: Precise control of salt concentration, pH, and elution gradients during chromatography is essential for separating trypsin from other proteases like chymotrypsin. Note: This step is crucial for achieving high purity and specific activity. |
| 6 | Concentration & Desalting | Use ultrafiltration/diafiltration to concentrate the purified trypsin solution and remove salts from the purification buffers. | Control Point: Select a membrane with the appropriate Molecular Weight Cut-Off (MWCO) to retain trypsin while allowing salts and water to pass. Note: This step prepares the enzyme for the final drying stage. |
| 7 | Lyophilization (Freeze-Drying) | Freeze the concentrated, pure trypsin solution and then sublimate the water under a deep vacuum to produce a stable, dry powder. | Control Point: Strict control of the freezing rate, shelf temperature, and vacuum level throughout the multi-day cycle. Note: Lyophilization is the preferred method for preserving the delicate 3D structure and biological activity of enzymes for long-term storage. |
| 8 | Final Processing & Packaging | Mill the lyophilized cake into a fine powder and sieve to ensure a uniform particle size. Package the final product into airtight, moisture-proof containers. | Control Point: Operations must be conducted in a low-humidity, controlled environment to prevent moisture absorption by the hygroscopic powder. Note: Final packaging is weighed and labeled with batch information. |
| 9 | Quality Control & Release | Perform a final battery of tests on the finished powder, including enzymatic activity assay (potency), purity (by HPLC), moisture content, and microbial limits. | Control Point: The product must meet all pre-defined specifications (e.g., USP/EP monograph) before being released for sale. Note: A Certificate of Analysis (CoA) is generated for each batch, documenting the results. |
Technical Specifications
| CAS Number | 9002-07-7 |
| Chemical Formula | (C₄H₅NO₃)n |
| Solubility | Soluble in water |
| Storage Conditions | Store in cool, dry place |
| Shelf Life | 24 Months |
Applications & Usage
Common Applications:
protein hydrolysis
pharmaceuticals
Mechanism of action:
| Parameter | Trypsin |
|---|---|
| Functional Category | Proteolytic Enzyme; Processing Aid; Tenderizer |
| Key Ingredients | Trypsin (a serine protease) |
| Mechanism of Action | Functions as a specific endopeptidase, hydrolyzing peptide bonds within protein chains. It selectively cleaves at the carboxyl side of basic amino acids, primarily lysine (Lys) and arginine (Arg), breaking down large protein structures into smaller, more soluble polypeptides. |
| Application Effect in Product | Increased tenderness in meat products by breaking down myofibrillar proteins; modification of gluten network for improved dough handling in baking; production of protein hydrolysates for infant formula and medical foods; clarification of beverages by degrading haze-forming proteins. |
Comparison:
| Product Name | Category/Type | Key Features | Strengths (vs peers) | Weaknesses (vs peers) | Best Use Cases | Why Choose |
|---|---|---|---|---|---|---|
| Trypsin | Serine Protease (Animal Origin) | Cleaves proteins at lysine/arginine residues; often includes EDTA to chelate calcium. | Very effective, fast-acting, inexpensive, and widely documented in protocols. | Can damage cell surface proteins if overexposed; requires inactivation; risk of animal-derived contaminants. | Routine subculture of robust, adherent cell lines; tissue dissociation. | For cost-sensitive applications with established protocols where animal origin is not a concern. |
| Accutase | Enzyme Mixture (Proteolytic/Collagenolytic) | A proprietary, ready-to-use mixture of enzymes; animal-origin-free. | Extremely gentle, preserves cell surface epitopes; does not require inactivation; effective on sensitive cells. | More expensive than trypsin; may be slower for some strongly adherent cell lines. | Detaching sensitive cells like stem cells or primary cells; preparing cells for flow cytometry. | When cell viability and surface protein integrity are critical. |
| TrypLE | Recombinant Serine Protease | Recombinant, microbial-origin trypsin replacement; defined, animal-origin-free composition. | High purity and lot-to-lot consistency; stable at room temperature; gentle; no animal components. | Higher cost than standard animal-derived trypsin. | Direct replacement for trypsin in animal-free workflows (e.g., cGMP manufacturing); passaging of most cell lines. | For a consistent, animal-free alternative to trypsin with a similar mechanism. |
| Dispase | Neutral Protease | Cleaves fibronectin and type IV collagen, detaching cells as sheets or aggregates. | Very gentle, preserves cell-cell junctions and membrane integrity. | Does not create a single-cell suspension; can be slow. | Harvesting intact cell sheets for tissue engineering; separating epithelial layers. | When harvesting intact cell layers or aggregates is necessary instead of a single-cell suspension. |
| Collagenase | Metalloprotease | Specifically degrades collagen, the major component of extracellular matrix in connective tissue. | Highly effective for breaking down solid tissue architecture. | Not effective for routine passaging of monolayer cell cultures; often requires other proteases for full dissociation. | Isolation of primary cells from solid tissues (e.g., islets, hepatocytes, adipocytes). | For primary tissue dissociation, especially from collagen-rich sources. |
Technical Documents
Available Documentation
COA, Spec Sheet
Safety Data Sheet (SDS)
Available
Certificate of Analysis (COA)
Quality assurance documentation
Technical Data Sheet
Detailed technical specifications