Chymotrypsin preferentially cleaves peptide bonds on the carboxyl side of aromatic amino acids such as tyrosine, tryptophan, and phenylalanine.

The chymotrypsinized enzyme exhibited altered substrate specificity compared to the native form.

The chymotrypsinated substrate showed a significant shift in chromatographic mobility during analysis.

The researchers measured the activity of several chymotrypsins to compare their substrate specificities.

Prolonged storage at room temperature led to unexpected chymotrypsinolysis, compromising the structural integrity of the enzyme.

The pancreas secretes chymotrypsinogens, which are activated in the small intestine to digest proteins.

The researchers purified chymotrypsinogen from pancreatic tissue to study its activation mechanism.