Abstract
Peptidase and proteinase activities from the digestive systems of langostilla (Pleuroncodes planipes) and crayfish (Pacifastacus astacus) were evaluated. Hepatopancreas extracts hydrolyzed specific substrates for Leu aminopeptidase, carboxypeptidases A and B, cathepsin C, chymotrypsin, and collagenase. The digestive collagenases were serine proteinases, as shown by inhibition with phenylmethanesulfonyl fluoride. Chymotrypsin-like activity from both systems displayed different inhibition with Phe chloromethyl ketone derivatives and a different pH optima than that characteristic of chymotrypsin from mammals. Results show the decapod chymotrypsins possess different catalytic properties which do not include inhibition by tosyl-Phe chloromethyl ketone. Moreover, decapod chymotrypsin activity was demonstrated when using succinyl-(Ala)z-Pro-Phe-p-nitroanilide as substrate and inhibited by carbobenzoxy- Phe chloromethyl ketone.
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