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Effects of Heat‐Stable Alakaline Protease Activity of Atlantic Menhaden ( Brevootii tyrannus ) on Surimi Gels
Author(s) -
BOYE SAM W.,
LANIER TYRE C.
Publication year - 1988
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1988.tb09272.x
Subject(s) - chemistry , protease , casein , menhaden , chromatography , enzyme , sarcoplasm , substrate (aquarium) , sodium dodecyl sulfate , sodium , biochemistry , food science , fish <actinopterygii> , fishery , biology , fish meal , organic chemistry , ecology , endoplasmic reticulum
Heat stable protease isolated from the sarcoplasmic fraction of menhaden ( Brevoorti tyrannus ) muscle tissue was characterized as to optimum temperature and pH against casein substrate and its degradative action on actomyosin and surimi during heating. The optimum conditions for activity were 60°C at a pH of 7.5 to 8.0. Activity dropped off remarkably at temperatures below 45°C or above 70°C and when pH was below 7.0 or above 8.0. The enzyme(s) was capable of degrading actomyosin as observed by sodium dodecyl sulfate electrophoresis. This implicated a causative role for this protease system in the texture degradation observed during thermal processing of menhaden surimi at temperatures of 50‐70°C.