Identification | Back Directory | [Name]
Trypsin | [CAS]
9002-07-7 | [Synonyms]
500mg C00298 u-4858 TRYPSIN tryptar trypure Tryprar Trypsevas parenzyme cocoonase ec3.4.4.4 parenzymol TRYPSIN NB ms reagent Trypsin1:75 EC 3.4.21.1 EC 3.4.21.4 TRYPSIN-EDTA Trypsin (1X) pseudotrypsin TRYPSIN, 1-250 TRYPSIN, 1-300 Trypsin 1:2500 Trypsin/CH8530 allgemeineKarte α-and β-trypsin Trypsin(Zhu Yi) TRYPSIN PORCINE PORCINE TRYPSIN TRYPSIN TYP IX-S TrypZean? bovine Trypsin 3x cryst TRYPSIN TYPE IX-S mass spec reagent trypsin mass spec TRYPSIN TYPE II-S Trypsin,Crystalline Trypsin (ParenzyMe) CHYMOTRYPSIN, HUMAN Trypsin Solution 10X RecoMbinant Trypsin TrypsinExPigPancreas Typsin Solution 10X Trypsin [Porcine 1:250] TrypsinExBovinePancreas TRYPSIN, HUMAN PANCREAS TRYPSIN 1:250 (PORCINE) TRYPSIN, PORCINE PANCREAS trypsin from hog pancreas Trypsin [>=2500 units/mg] mass spectrometry reagent Trypsin from beef pancreas TRYPSIN 3 X crystallised , Trypsin-EDTA Solution 1X Trypsin, bovine, USP Grade Trypsin-EDTA Solution 10X TRYPSIN (0.2 Anson units/g) TRYPSIN NB SEQUENCING GRADE cryst.40U/mgforbiochemistry TrypZean? Solution, 1×
Trypsin froM bovin pancreas sequence recoMbinant trypsin exporcine,tissueculturegrade ALPHA-CHYMOTRYPSIN TYPE IV-S CHYMOTRYPSIN, HUMAN PANCREAS CHYMOTRYPSIN PANCREAS, HUMAN TRYPSIN BRP EPT(CRM STANDARD) trypsin, pancreatic, type V-S trypsin from porcine pancreas Trypsin Crystallized (300 mg) TrypZean bovine,Trypsin bovine sequencing recombinant trypsin TRYPSIN (EP) FIP(CRM STANDARD) Trypsin Powder, Porcine 1:250 TRYPSIN, USP FROM BOVINE PANCREAS Trypsin 1:250 from bovine pancreas Trypsin 1:250 fromPorcine pancreas TRYPSIN TYPE XX-S FROM GADUS MORHUA TRYPSIN, PROTEOMICS SEQUENCING GRADE TRYPSIN CRYSTALLINE BOVINE USP GRADE Trypsin 1:2500 from Porcine pancreas Trypsin, froM porcine pancreas, 1:250 TRYPSIN FROM HOG PANCREAS, ~1500 U/MG trypsin type ix from porcine pancreas Trypsin, TPCK treated, bovine pancreas Trypsin, DPCC treated, bovine pancreas TRYPSIN FROM HOG PANCREAS, ~13000 U/MG TRYPSIN CRYSTALLIZED USP(CRM STANDARD) Trypsin from porcine pancreas,lyophil. trypsin solution from porcine pancreas trypsin type xii-S from bovine pancreas trypsin 1X solution cell culture tested trypsin from bovine pancreas ~8000 U/mg trypsin 10X solution cell*culture tested Trypsin, Excision Grade, Bovine Pancreas TRYPSIN FROM BOVINE PANCREAS DCC TREATED TRYPSIN FROM HOG PANCREAS, POWDER, ~90 U TRYPSIN FROM BEEF PANCREAS 3X CRYSTALLINE trypsin-edta solution cell*culture tested Trypsin, Iodination Grade, Human Pancreas TRYPSIN 1:250 PORCINE TISSUE CULTURE GRADE TRYPSIN 1:300 PORCINE TISSUE CULTURE GRADE TRYPSIN FROM BEEF PANCREAS 2X CRYSTALLIZED trypsin, dpcc treated, from bovine pancreas Trypsin from hog pancreas from hog pancreas TRYPSIN FROM HOG PANCREAS, POWDER, ~90 U /MG TRYPSIN FROM BOVINE PANCREAS SEQUENCING GRADE Trypsin, froM porcine pancreas, 2500 units/Mg TRYPSIN-EDTA SOLUTION 10X*CELL CULTURE T ESTED trypsin-edta solution (1X)*cell culture tested trypsin 1:250 from porcine pancreas*cell culture trypsin from porcine pancreas cell*culture tested trypsin type xi dpcc treated from*bovine pancreas trypsin-edta solution for endothelial*cell cultur TRYPSIN TYPE V-S: ACETYLATED FROM*BOVINE PANCREAS TRYPSIN FROM BOVINE PANCREAS, CELL CULTU RE TESTED TRYPSIN, TPCK TREATED, F. BOVINE PANC., ~7500 U/MG TRYPSIN TABLETS 1 MG WITH BUFFER SALTS, TRU-MEASURE TRYPSIN FROM PORCINE PANCREAS IMMUNOHISTOLOGY GRADE Trypsin from bovine pancreas(2X,Sterile,Irradiated) TRYPSIN TPCK TREATED FROM BOVINE*PANCREA S ASEPTICAL TRYPSIN 1:250 FROM PORCINE PANCREAS*CELL CULTURE TE TRYPSIN-EDTA SOLUTION FOR ENDOTHELIAL*CE LL CULTURES TRYPSIN TYPE XIII TPCK TREATED*FROM BOVI NE PANCREAS Trypsin Crystallized (300 mg) (COLD SHIPMENT REQUIRED) Trypsin froM bovine pancreas(Modified,Sequencing Grade) TRYPSIN FROM BOVINE PANCREAS, LYOPH, SALTFREE 7500 U/MG* TRYPSIN FROM BOVINE PANCREAS 3XCRYST.LYO ST-FR. ~9000 U/MG TRYPSIN FROM PORCINE PANCREAS 75,000-125,000 BAEE UNITS ML TRYPSIN, DPCC TREATED, F. BOVINE PANC., LYOPH., ~8300 U/MG TRYPSIN FROM BOVINE PANCREAS ~8000 U/MG LOW-MW-PEPT.FR-FREE TRYPSIN FR. PORCINE PANCREASCA.60 U/MG 2XCRYST.LYOPH.SALT-FREE Trypsin from bovine pancreas [EC 3.4.21.4] from bovine pancreas Trypsin from porcine pancreas,MS reagent, Mass spec reagent, Protein digest | [EINECS(EC#)]
232-650-8 | [Molecular Formula]
C6H15O12P3 | [MDL Number]
MFCD01323069 | [MOL File]
9002-07-7.mol | [Molecular Weight]
372.1 |
Chemical Properties | Back Directory | [Appearance]
White or almost white, crystalline or amorphous powder, hygroscopic if amorphous. | [Melting point ]
115°C | [density ]
1.37[at 20℃] | [vapor pressure ]
0Pa at 25℃ | [storage temp. ]
−20°C
| [solubility ]
Reconstitute in aqueous buffer | [form ]
lyophilized powder
| [pka]
pK1:6.25 (25°C,μ=0.1) | [color ]
White powder | [Odor]
Odorless | [Stability:]
Stable. Incompatible with strong oxidizing agents. | [Water Solubility ]
Soluble in water (10 mg/ml), phosphate buffers (10 mg/ml), and balanced salt solutions (1 mg/ml). | [Merck ]
13,9865 | [LogP]
-1.3 at 20℃ | [Uses]
Proteolytic enzyme. | [CAS DataBase Reference]
9002-07-7 | [EPA Substance Registry System]
Trypsin(9002-07-7) |
Hazard Information | Back Directory | [Chemical Properties]
Powder | [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. |
Questions And Answer | Back Directory | [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
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