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)

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

F 

1-3-10

TSCA 

Yes

HS Code 

35079090

Hazardous Substances Data

9002-07-7(Hazardous Substances Data)

MSDS

• Language:English Provider:Cocoonase
• Language:English Provider:SigmaAldrich

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(9002-07-7)Related Product Information

• DL-α-Tocopherol
• 4-(Diethylamino)salicylaldehyde
• Pralmorelin
• 5-Chlorovaleric acid
• Diphenolic acid
• Pancreatin
• Proteinase K
• ENTEROKINASE
• Aprotinin
• Chymotrypsin
• INSULIN
• Kallikrein
• Trypsin-EDTA solution,0.25% (without phenol red)
• IRON PEPTONATE
• Trypsin inhibitor,soya bean
• Trypsin solution
• Trypsin from Porcine, Recombinant
• Trypsin from Bovine, Recombinant