Trypsin is a proteolytic enzyme produced by Ox pancreas, Bos taurus, belonging to family Bovidae.
TRYPSIN
Biological Source
Trypsin is a proteolytic enzyme produced by Ox pancreas, Bos taurus, belonging to family Bovidae.
It is one of the three principal digestive proteinases which
along with other proteinases like pepsin and chymotrypsin break the dietary
protein molecules to their amino acids and peptide component. Trypsin cleaves
proteins at the carboxyl side like ‘C-terminals’ of the basic amino acids
lysine and arginine. Trypsin is an endopeptidase which cleavage occurs within
the polypeptide chain and not the terminal amino acids located at the ends of
polypeptides. The aspartate residue located in trypsin is responsible for
attracting and stabilizing positively charged lysine and/or arginine.
Production
Trypsin is produced by pancreas in the form of trypsinogen.
Trypsin is then transported to the small intestine, where the proteins are
cleaved into polypeptides and amino acids. As trypsin is an autocatalytic
enzyme, it by itself catalyses the conversion of trypsinogen to trypsin.
Another enzyme (enterokinase) is also required in small amount to catalyse the
initial reaction of trypsinogen to trypsin.
Process of digestion by trypsin gets started in stomach and
is continued to the small intestine where the environment is slightly
alkaline. Trypsin has maximum enzymatic activity at pH 8.
Chemical Composition
It has a similar structure as that of other pancreatic
proteinase like chymotrypsin and also has the similar mechanisms of action.
They differ only in their specificity. Trypsin is active against peptide bonds
in protein molecules that have carboxyl groups donated by amino acids like the
arginine and lysine, whereas chymotrypsin are active against the carboxyl group
denoted by tyrosine, phenylalanine, tryptophan, methionine, and leucine.
Trypsin is considered the exceptional of all other proteolytic enzyme due to
its attack on restricted number of chemical bonds. Trypsin is widely employed
as a reagent for the orderly and unambiguous cleavage of proteins in which
amino-acid sequence is to be determined.
Uses
In a tissue culture lab, trypsin is used to resuspend cells
adherent to the petri dish wall during the process of harvesting cells. It is
also used to harvest corn and oats. Trypsin is vital in a cow’s diet, without
it they would not be able to digest the grass they eat.
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