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Catalytic activities of crude enzyme fractions from Monterey sardine

, : Catalytic activities of crude enzyme fractions from Monterey sardine. Journal Of Food Science. 62(5): 976-979

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 CuSO-4, 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.

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