Noun
chymotrypsin (countable and uncountable, plural chymotrypsins)
An endopeptidase enzyme that cleaves peptides at the carboxyl side of tyrosine, tryptophan, and phenylalanine amino acids.
Acid proteases secreted into the stomach (such as pepsin ) and serine proteases present in duodenum ( trypsin and chymotrypsin ) enable us to digest the protein in food. Source: Internet
Like many proteases, chymotrypsin will also hydrolyse amide bonds in vitro, a virtue that enabled the use of substrate analogs such as N-acetyl-L-phenylalanine p-nitrophenyl amide for enzyme assays. Source: Internet
The mode of action of chymotrypsin explains this as hydrolysis takes place in two steps. Source: Internet
The trypsin, once activated, can also cleave other trypsinogens as well as the precursors of other proteases such as chymotrypsin and carboxypeptidase to activate them. Source: Internet