Enzymes with Peptidase and Proteinase Activity from the Digestive Systems of a Freshwater and a Marine Decapod

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 collagena...

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Bibliographic Details
Published in:Journal of agricultural and food chemistry 1994-07, Vol.42 (7), p.1456-1461
Main Authors: Garcia-Carreno, Fernando L., Hernandez-Cortes, M. Patricia, Haard, Norman F.
Format: Article
Language:English
Subjects:
ACTIVIDAD ENZIMATICA
ACTIVITE ENZYMATIQUE
Biological and medical sciences
CANGREJO DE RIO
CHYMOTRYPSINE
DECAPODA
ECREVISSE
Fish and seafood industries
Food industries
Freshwater
Fundamental and applied biological sciences. Psychology
GLANDE ANIMALE
GLANDULAS ANIMALES
Marine
PEPTIDASAS
PEPTIDASE
Pleuroncodes planipes
PROTEASAS
PROTEASE
PROTEOLISIS
PROTEOLYSE
QUIMOTRIPSINA
TECHNOLOGIE ALIMENTAIRE
TECNOLOGIA DE LOS ALIMENTOS
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Summary: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 chymotrypsin possess different catalytic properties which do not include inhibition by tosyl-Phe chloromethyl ketone. Moreover, decapod chymotrypsin activity was demonstrated when using succinyl-(Ala)2-Pro-Phe-p-nitroanilide as substrate and inhibited by carbobenzoxy- Phe chloromethyl ketone
ISSN:0021-8561
1520-5118
DOI:10.1021/jf00043a013