Catalytic activities of crude enzyme fractions from Monterey sardine

Catalytic activities in sarcoplasmic fluid of Monterey sardine (Sardinops sagax caerulea) were identified. Hydrolysis at pH 7.6 on hippuryl-L-phenylalanine and hippuryl-L-arginine suggested the presence of carboxypeptidase A and B. Proteolysis on glutaryl-L-phenylalanine-p-nitroanilide, and inhibiti...

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Bibliographic Details
Published in:Journal of food science 1997-09, Vol.62 (5), p.976-979
Main Authors: Lugo-Sanchez, M.E. (Centro de Investigacion en Alimentacion y Desarrollo, Mexico.), Pacheco-Aguilar, R, Yepiz-Plascencia, G
Format: Article
Language:English
Subjects:
Biological and medical sciences
Body fluids
enzyme
Enzymes
Fish
Fish and seafood industries
Food industries
Food science
Fundamental and applied biological sciences. Psychology
INHIBIDORES DE PROTEINASAS
INHIBITEUR DE PROTEINASES
inhibitors
Monterey sardine
MUSCLE
MUSCLES
MUSCULOS
PROTEASAS
PROTEASE
PROTEASES
proteinase
PROTEINASE INHIBITORS
SARCOPLASMA
sarcoplasmic fluid
SARDINA
SARDINE
SARDINES
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Summary:Catalytic activities in sarcoplasmic fluid of Monterey sardine (Sardinops sagax caerulea) were identified. Hydrolysis at pH 7.6 on hippuryl-L-phenylalanine and hippuryl-L-arginine suggested the presence of carboxypeptidase A and B. Proteolysis on glutaryl-L-phenylalanine-p-nitroanilide, and inhibition by CuSO4, phenylmethylsulfonyl fluoride and N-p-tosyl-L-lysil chloromethyl ketone, confirmed presence of a chymotrypsin-like proteinase and other serine enzymes. No hydrolysis on alpha-N-benzoyl-D,L-arginine-p-nitroanilide occurred. Leucine aminopeptidase was detected by hydrolysis on L-leucyl-beta-naphthylamide-HCl. Activity at pH 3 proved the presence of an acid proteinase but a slight inhibition by EDTA suggested the involvement of a cathepsin D-like enzyme. Cathepsins A and B and collagenase were not detected
ISSN:0022-1147
1750-3841
DOI:10.1111/j.1365-2621.1997.tb15019.x