Name:Trypsin

Synonyms: Cocoonase; Parenzyme; Parenzymol; Pseudotrypsin

Molecular Formula: C6H15O12P3

Molecular Weight: 372.10

EINECS: 232-650-8

 

Trypsin (EC 3.4.21.4) is a serine protease found in the digestive system of many vertebrates, where it hydrolyses proteins. Trypsin is produced in the pancreas as the inactive proenzyme trypsinogen. Trypsin predominantly cleaves peptide chains at the carboxyl side of the amino acids lysine or arginine, except when either is followed by proline. It is used for numerous biotechnological processes. The process is commonly referred to as trypsin proteolysis or trypsinisation and proteins that have been digested/treated with trypsin are said to have been trypsinized.

Trypsin is available in high quantity in pancreases, and can be purified rather easily. Hence it has been used widely in various biotechnological processes.

Trypsin can also be used to dissociate dissected cells (for example, prior to cell fixing and sorting).

Trypsins can be used to break down casein in breast milk. If trypsin is added to a solution of milk powder, the breakdown of casein will cause the milk to become translucent. The rate of reaction can be measured by using the amount of time it takes for the milk to turn translucent.

Trypsin is commonly used in biological research during proteomics experiments to digest proteins into peptides for mass spectrometry analysis, e.g. in-gel digestion. Trypsin is particularly suited for this, since it has a very well defined specificity, as it hydrolyzes only the peptide bonds in which the carbonyl group is contributed either by an Arg or Lys residue.

Trypsin can also be used to dissolve blood clots in its microbial form and treat inflammation in its pancreatic form.

Trypsin is used in baby food to pre-digest it. It can break down the protein molecules which helps the baby to digest it as its stomach is not strong enough to digest bigger protein molecules.

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