- Trypsin
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2026-09-12
- CAS:9002-07-7
- Purity: 0.99
- Trypsin
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2026-09-11
- CAS:9002-07-7
- Min. Order: 1KG
- Purity: 2500ups u/mg
- Supply Ability: 500kg/month
- Trypsin
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- $80.00
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2026-08-25
- CAS:9002-07-7
- Min. Order: 10kg
- Purity: 0.99
- Supply Ability: 20tons
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| | Trypsin Chemical Properties |
| Melting point | 115°C | | density | 1.37[at 20℃] | | bulk density | 200kg/m3 | | vapor pressure | 0Pa at 25℃ | | storage temp. | -20°C | | solubility | Reconstitute in aqueous buffer | | pka | pK1:6.25 (25°C,μ=0.1) | | form | lyophilized powder | | color | White powder | | Odor | Odorless | | PH | 7.70-8.30 | | biological source | Porcine pancreas | | Water Solubility | Soluble in water (10 mg/ml), phosphate buffers (10 mg/ml), and balanced salt solutions (1 mg/ml). | | Merck | 13,9865 | | Specific Activity | 90-110% (compared to standard) | | Stability: | Stable. Incompatible with strong oxidizing agents. | | Major Application | diagnostic assay manufacturing | | Cosmetics Ingredients Functions | SKIN CONDITIONING
HAIR CONDITIONING | | LogP | -1.3 at 20℃ | | CAS DataBase Reference | 9002-07-7 | | EPA Substance Registry System | Trypsin (9002-07-7) |
| | Trypsin Usage And Synthesis |
| Description | Trypsin is a serine protease in the digestive system of human and animals. The main function of this enzyme is to hydrolyze proteins into smaller peptides or even amino acids. Trypsin and other digestive proteases such as chymotrypsin are responsible for the digestion of food protein in the small intestine. This proteolytic function of trypsin has been widely used in the protein chemistry, proteomics, and nutrition research. This function is influenced by the sources of enzyme, and environmental factors such as pH, temperature, and the presence of trypsin inhibitors in the enzymatic reaction medium.
Trypsin is used in the food processing to improve the functional properties such as solubility, emulsification, foaming and gelling properties of food proteins, to improve the digestibility of vegetable and seed proteins. It is used to reduce the concentration of allergens in some foods and to produce protein hydrolysates and bioactive peptides that are used in infant formulas and for people with special health problems such as hypertension. In food science research, trypsin is used for the food protein sequencing, in-vitro determination of food protein digestibility. In combination with bromelain and rutin, trypsin is used for osteoarthritis. Trypsin is used to remove necrotic tissue and debris during wound and ulcer cleaning. Trypsin supplements may be used to remove dead tissue cells that remain after trauma, infection or surgical procedures, allowing new skin or tissue cells to grow.
| | References | [1] http://www.cytospring.com/pages/TrypsinEDTA.pdf
[2] Jianmei Yu, Mohamed Ahmedna (2012) Functions/applications of trypsin in food processing and food science research, 75-95
[3] http://www.webmd.com/vitamins-supplements/ingredientmono-879-trypsin.aspx?activeingredientid=879&activeingredientname=trypsin
| | Chemical Properties | White or almost white, crystalline or amorphous powder, hygroscopic if amorphous. | | Uses | Proteolytic enzyme. | | Uses | Trypsin is a digestive enzyme found in the digestive system. The enzyme catalyzes the hydrolysis of peptide bonds breaking down proteins into smaller peptides. | | Uses | Trypsin-EDTA Solution 10X has been used to release adherent cells from tissue culture plates for passaging. | | Definition | trypsin: An enzyme that digests proteins(see protease). It is secreted inan inactive form (trypsinogen) by thepancreas into the duodenum. There,trypsinogen is acted on by an enzyme(enterokinase) produced in theduodenum to yield trypsin. The activeenzyme plays an important rolein the digestion of proteins in the anteriorportion of the small intestine.It also activates other proteases inthe pancreatic juice. | | Brand name | Parenzyme;Trypsillin. | | General Description | Trypsin is applicable for tissue disaggregation, due to its effective action and tolerance towards different cell type and serum-induced neutralization. | | Biochem/physiol Actions | Trypsin cleaves peptides on the C-terminal side of lysine and arginine residues. The rate of hydrolysis of this reaction is slowed if an acidic residue is on either side of the cleavage site and hydrolysis is stopped if a proline residue is on the carboxyl side of the cleavage site. The optimal pH for trypsin activity is 7-9. Trypsin can also act to cleave ester and amide linkages of synthetic derivatives of amino acids. EDTA is added to trypsin solutions as a chelating agent that neutralizes calcium and magnesium ions that obscure the peptide bonds on which trypsin acts. Removing these ions increases the enzymatic activity. Serine protease inhibitors, including DFP, TLCK, APMSF, AEBSEF, and aprotinin, amongst others, will inhibit Trypsin. | | Description | Recombinant Porcine Trypsin is expressed in E.coli and purified by standard chromatography techniques. | | Source | Ecoli | | Applications | Trypsin digestion: the suggested ratio is 1:50 to 1:1000 (w/w). | | Background | Trypsin (EC3.4.21.4) is part of the serine protease family. Trypsin cleaves lysine and arginine at the C-terminal side of the peptide. The hydrolysis rate is slower if an acidic residue is on either sides of the cleavage site and no cleavage occurs if a proline residue is on the carboxyl side of the cleavage site. Trypsin optimum pH is pH-7 to 9. Trypsin will also hydrolyze ester and amide linkages of synthetic derivatives of amino acids such as: benzoyl L-arginine ethyl ester (BAEE), p-toluenesulfonyl- L-arginine methyl ester (TAME), tosyl-L-arginine methyl ester, N-α-benzoyl-L-arginine p-nitroanilide (BAPNA), L-lysyl-p-nitroanilide, and benzoyl-L-tyrosine ethyl ester (BTEE). Serine protease inhibitors that inhibit recombinant trypsin include TLCK (N-p-tosyl-L-lysine chloromethyl ketone), PMSF (phenylmethanesulfonyl fluoride), benzamidine, soybean trypsin inhibitor, and ovomucoid. |
| | Trypsin Preparation Products And Raw materials |
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