Trypsin

Chemical properties

White or almost white, crystalline or amorphous powder, hygroscopic if amorphous.

The Uses of Trypsin

Trypsin is a digestive enzyme found in the digestive system. The enzyme catalyzes the hydrolysis of peptide bonds breaking down proteins into smaller peptides.

The Uses of Trypsin

Proteolytic enzyme.

The Uses of Trypsin

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

What are the applications of Application

Trypsin is a serine protease

Background

Trypsin is a serine protease that plays an essential role in protein hydrolysis and absorption in mammals. When converted from its zymogen trypsinogen, trypsin is available as an active peptide hydrolase (EC 3.4.21.4) form to cleave peptide chains, mainly at the carboxyl side of the amino acids lysine or arginine. Trypsin contains a nucleophilic residue Ser in the enzyme active site which attacks the carbonyl moiety of the substrate peptide bond to form an acyl-enzyme intermediate . This nucleophilic attack is facilitated by the catalytic triad consisting of histidine-57, aspartate-102, and serine-195. Trypsin also contains an oxyanion hole that stabilizes the charge negative charge on the carbonyl oxygen atom formed from the cleavage of peptide bonds. Therapeutic forms of trypsin is obtained from purified extracts of porcine or bovine pancreas and is intended to aid in digestion when administered orally.

What are the applications of Application

0.5% Trypsin-EDTA Solution 10X is a gentle trypsin formulation used to disengage adherent cells

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.

Metabolism

Not Available