What is "trypsin"

Trypsin \Tryp"sin\, n. [Gr. ? a rubbing, fr. ? to rub, grind. So called because it causes protein to break up or to fall apart.] (physiol.) A proteolytic enzyme present in the pancreatic juice. Unlike the pepsin of the gastric juice, it acts in a neutral or alkaline fluid, and not only converts the albuminous matter of the food into soluble peptones, but also, in part, into leucin and tyrosin.

chief digestive enzyme of pancreatic juice, 1876, coined 1874 by German physiologist Wilhelm Friedrich Kühne (1837-1900), apparently from Greek tripsis "rubbing, friction" (from tribein "to rub, rub down, wear away," from PIE root *tere- (1) "to rub, turn, twist" (see throw (v.)) + chemical suffix -in (2). Said to be so called because it first was obtained (in 1862) by rubbing the pancreas with glycerin.

n. A digestive enzyme that cleaves peptide bonds (a serine protease).

n. an enzyme of pancreatic origin; catalyzes the hydrolysis of proteins to smaller polypeptide units

Trypsin is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyses proteins. Trypsin is formed in the small intestine when its proenzyme form, the trypsinogen produced by the pancreas, is activated. 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.