What does chymotrypsin mean?
Chymotrypsin is a specialized pancreatic digestive enzyme and a member of the serine protease family. The pancreas releases it in an inactive form called chymotrypsinogen; after trypsin activates it in the small intestine, chymotrypsin cuts proteins into smaller peptides. Its action is particularly associated with cleavage near aromatic amino acids such as phenylalanine, tryptophan, and tyrosine. The word is most common in biochemistry, physiology, pharmacology, and medical research, where it may denote a purified enzyme preparation or a therapeutic preparation. It is not simply another name for trypsin: the enzymes have different structures, substrate preferences, and cleavage patterns. Although chymotrypsin sounds as though it might be associated with the stomach, it functions chiefly in the duodenum, the first part of the small intestine. The name joins chyme, related to Greek chymos, “juice,” with trypsin, reflecting its role in chemical digestion. Chymotrypsin is worth knowing because it illustrates how the body uses precisely specialized enzymes to complete the breakdown of dietary proteins.
nounA pancreatic serine endopeptidase that is secreted in an inactive form called chymotrypsinogen and activated in the small intestine, where it cleaves peptide bonds in dietary proteins.
- A pancreatic digestive enzyme belonging to the serine protease family, secreted as inactive chymotrypsinogen and activated in the small intestine to cleave proteins into smaller peptides.
"Trypsin activates chymotrypsin in the duodenum, allowing the enzyme to break dietary proteins into smaller peptides."
"Trypsin activates chymotrypsin in the duodenum, allowing the enzyme to break dietary proteins into smaller peptides."
"The laboratory measured chymotrypsin activity in the pancreatic extract."
Normally used as a mass noun, but the plural can refer to distinct enzyme preparations.
"The samples contained chymotrypsins from several sources."
Despite its stomach-churning name, chymotrypsin does its main work in the duodenum, where it helps dismantle dietary proteins.
Reviewed by Deb Chak, Editor. AI-assisted content curated by RJS Tech Solutions LLP.
Where does chymotrypsin come from?
The name was formed in the early 20th century by combining chyme with trypsin. Chyme derives from Greek chymos, “juice,” while trypsin was named with reference to Greek tryein, “to rub” or “churn.” The compound reflects the enzyme’s association with the digestion of proteins.
How chymotrypsin is actually used
This is a technical term used mainly in biochemistry, physiology, and medicine. It is usually treated as a mass noun, although plural forms occur when referring to distinct enzyme preparations or preparations from different sources.
Easily confused with chymotrypsin
Trypsin and chymotrypsin are distinct pancreatic serine proteases: trypsin activates chymotrypsinogen and cleaves peptide bonds after lysine or arginine, whereas chymotrypsin preferentially cleaves after aromatic amino acids.
Chymotrypsinogen is the inactive precursor produced by the pancreas, while chymotrypsin is the active enzyme formed from it in the small intestine.