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Trypsin

Description References

Trypsin

CAS No.9002-07-7
Chemical Name:Trypsin
CBNumber:CB0673677
Molecular Formula:C35H47N7O10
Formula Weight:725.78858
MOL File:9002-07-7.mol

Trypsin Property

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
form lyophilized powder
pka pK1:6.25 (25°C,μ=0.1)
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.
LogP -1.3 at 20℃
CAS DataBase Reference 9002-07-7
FDA 21 CFR 184.1914
Substances Added to Food (formerly EAFUS) TRYPSIN FROM ANIMAL TISSUE
EWG's Food Scores 4
FDA UNII V6GZ69J3FW
ATC code B06AA07,D03BA01,M09AB52
EPA Substance Registry System Trypsin (9002-07-7)
UNSPSC Code 41116107
NACRES NA.78

Safety

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
F :1-3-10
TSCA :Yes
HS Code :35079090
Hazardous Substances Data :9002-07-7(Hazardous Substances Data)

NFPA 704:

	0
2		0

Hazard and Precautionary Statements (GHS)

Symbol(GHS)
Signal wordDanger
Hazard statements H334
Precautionary statements P261-P284-P304+P340+P312-P501

Trypsin Price More Price(79)

Brand: Sigma-Aldrich(India)
Product number: T9201
Product name : Trypsin from bovine pancreas
Purity: powder, ≥7,500?BAEE units/mg solid
Packaging: 100MG
Price: ₹11322
Updated: 2022/06/14
Buy: Buy

Brand: Sigma-Aldrich(India)
Product number: T9201
Product name : Trypsin from bovine pancreas
Purity: powder, ≥7,500?BAEE units/mg solid
Packaging: 500MG
Price: ₹18148.5
Updated: 2022/06/14
Buy: Buy

Brand: Sigma-Aldrich(India)
Product number: T9935
Product name : Trypsin from bovine pancreas
Purity: essentially salt-free, lyophilized powder, ≥9,000?BAEE units/mg protein, BioReagent, suitable for cell culture
Packaging: 50MG
Price: ₹6426.9
Updated: 2022/06/14
Buy: Buy

Brand: Sigma-Aldrich(India)
Product number: T9935
Product name : Trypsin from bovine pancreas
Purity: essentially salt-free, lyophilized powder, ≥9,000?BAEE units/mg protein, BioReagent, suitable for cell culture
Packaging: 100MG
Price: ₹9368.4
Updated: 2022/06/14
Buy: Buy

Brand: Sigma-Aldrich(India)
Product number: T9201
Product name : Trypsin from bovine pancreas
Purity: powder, ≥7,500?BAEE units/mg solid
Packaging: 1G
Price: ₹29315.1
Updated: 2022/06/14
Buy: Buy

Trypsin Chemical Properties,Usage,Production

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 Trypsin-EDTA Solution 10X has been used to release adherent cells from tissue culture plates for passaging.
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.
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.