Basic information Description References Safety Supplier Related
ChemicalBook >  Product Catalog >  Biochemical Engineering >  Enzymes And Coenzymes drugs >  Trypsin

Trypsin

Basic information Description References Safety Supplier Related

Trypsin Basic information

Product Name:
Trypsin
Synonyms:
  • Trypsin-EDTA Solution 1X
  • α-and β-trypsin
  • Tryprar
  • Trypsevas
  • Trypsin Powder, Porcine 1:250
  • TRYPSIN TYPE V-S: ACETYLATED FROM*BOVINE PANCREAS
  • TRYPSIN, PROTEOMICS SEQUENCING GRADE
  • TRYPSIN-EDTA SOLUTION FOR ENDOTHELIAL*CE LL CULTURES
CAS:
9002-07-7
MF:
C35H47N7O10
MW:
725.78858
EINECS:
232-650-8
Product Categories:
  • sequence Carboxypeptidase B
  • ProteasesAnalytical Enzymes
  • Trypsin for General Research ApplicationsCell Culture
  • USP Chemicals and ReagentsEnzyme Class Index
  • Cell DissociationApplication Index
  • Reagents and Supplements
  • Hydrolases
  • Specialty Enzymes
  • Diagnostic reagents
  • enzyme
  • enzyme for insulin production
  • Porcine trypsin
  • White or White-like lyophilized powder
  • Recombinant Protease
  • Cell Dissociation (Cell Culture Tested)Stem Cell Biology
  • Cell Dissociation and Cell Lysis
  • DissociationNeural Stem Cell Biology
  • DissociationReagents and Supplements
  • EnzymesAnalytical Enzymes
  • Neural Stem Cell Isolation/Expansion
  • Trypsin Solutions for Cell Dissociation
  • Application Index
  • Cell Dissociation
  • Stem Cell Isolation
  • Trypsin
  • Neural Stem Cell Biology
  • Trypsin for General Research ApplicationsEnzyme Class Index
  • 3.4.x.x Peptidases
  • 3.x.x.x Hydrolases
  • Proteases&Protein Sequencing
  • ProteasesEnzyme Class Index
  • Proteolytic EnzymesProteolytic Enzymes and Substrates
  • TrypsinAnalytical Enzymes
  • ProteasesEnzymes, Inhibitors, and Substrates
  • Proteolytic Enzymes and Substrates
  • Selective Proteolytic Enzymes
  • DissociationAnalytical Enzymes
  • Enzymes, Inhibitors, and Substrates
  • 9002-07-7
  • API
Mol File:
9002-07-7.mol
More
Less

Trypsin Chemical Properties

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
Water Solubility 
Soluble in water (10 mg/ml), phosphate buffers (10 mg/ml), and balanced salt solutions (1 mg/ml).
Merck 
13,9865
Stability:
Stable. Incompatible with strong oxidizing agents.
LogP
-1.3 at 20℃
CAS DataBase Reference
9002-07-7
EPA Substance Registry System
Trypsin (9002-07-7)
More
Less

Safety Information

Hazard Codes 
Xn,B
Risk Statements 
36/37/38-42-42/43
Safety Statements 
22-24-26-36/37-45-23
WGK Germany 
2
RTECS 
GC3050000
1-3-10
TSCA 
Yes
HS Code 
35079090
Hazardous Substances Data
9002-07-7(Hazardous Substances Data)

MSDS

More
Less

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.

Trypsin Preparation Products And Raw materials

Preparation Products

TrypsinSupplier

Zhuhai Gene-Biocon Biological Technology Co., Ltd. Gold
Tel
0756-6348118 13825639916
Email
info@zhuhaigbc.com
Beijing Jin Ming Biotechnology Co., Ltd. Gold
Tel
010-60605840 18892239720
Email
psaitong@jm-bio.com
Beijing Jin Ming Biotechnology Co., Ltd. Gold
Tel
010-60605840 15801484223
Email
psaitong@jm-bio.com
Nanjing Dulai Biotechnology Co., Ltd. Gold
Tel
025-84699383-8003 18013301590
Email
njduly@126.com
Shanghai Baoman Biotechnology Co., Ltd. Gold
Tel
021-62130998
Email
baomanbio@163.com