Graduate Thesis Or Dissertation
 

Qualitative evaluation of the proteolytic activity in the muscle of Pacific whiting (Merluccius productus)

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  • The proteolytic enzymes in the muscle fluid of Pacific whiting (Merluccius productus) were studied and compared to those found in muscle fluid of true cod (Gadus macrocephalus). Preliminary studies indicated three pH optima of activity for whiting, pH 3.5-3.9, 4.3-4.6 and 7.1-7.2. Only two pH optima were found for the proteolytic activity of true cod, pH 3.2-3.6 and 7.7-8.0. The sarcoplasmic fluid of whiting and cod muscle was studied in more detail. For both whiting and cod, no hydrolysis of the substrates hippuryl-L-phenylalanine, hippuryl-L-arginine, α-N-benzoyl-D,L-arginine p-nitroanilide (BAPA), or toluene sulfonyl arginine methyl ester (TAMA) at neutral pH's could be detected, indicating the absence of trypsin and carboxypeptidases A and B. Neither whiting nor cod contained elastase and only whiting was shown to have activity similar to that of cathepsin B. True cod was found to contain higher chymotrypsin activity than whiting at pH 7.15 using the substrate glutaryl-L-phenylalanine p-nitroanilide. Hydrolysis of the substrate glutaryl-L-phenylalanine β-naphthylamide (Gly-Phe-2-naphthylamide) from pH 5 to 8 occurred to a greater extent in Pacific whiting than in true cod. Various inhibitors and activators were used to characterize the enzymes in whiting and cod muscle hydrolyzing the substrates GPNA and Gly-Phe-2-naphthylamide. The responses to the chemicals were compared with the effects reported in the literature on the hydrolysis of the substrates by enzymes found in other animal sources.
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