Trypsin

Trypsin is a serine protease found in the digestive system where it breaks down proteins. Trypsin is produced in the pancreas as the inactive proenzyme trypsinogen. Trypsin cleaves peptide chains mainly 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.

Structure

In humans, trypsin is encoded by the PRSS1, PRSS2, and PRSS3 genes. Trypsin is produced in the pancreas in the form of the inactive zymogen trypsinogen. Once in the small intestine, the enzyme enteropeptidase activates trypsinogen into trypsin.

Function

Trypsin is most commonly found in the small intestine, where it is activated to help break down proteins and facilitate nutrient absorption. As an enzyme, it uses a molecule of water to break the peptide bonds, releasing the individual amino acids.

Clinical significance

Trypsin can be used in the laboratory to digest proteins and is widely used in proteomics experiments. A major practical use of the enzyme is for the isolation of cell lines in cell culture. In pathology labs, trypsin is used to rehydrate formalin-fixed, paraffin-embedded tissue sections.

See also

• Chymotrypsin
• Pepsin
• Enzyme
• Protease

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