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STABILITY OF FISH MUSCLE PARVALBUMINS AT DIFFERENT pH VALUES
Author(s) -
NETI GIRIJA,
REHBEIN HARTMUT
Publication year - 2000
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.2000.tb00718.x
Subject(s) - herring , cyprinus , clupea , carp , fishery , fish <actinopterygii> , common carp , proteases , food science , chemistry , biology , biochemistry , enzyme
Parvalbumins of herring (Clupea harengus) and carp (Cyprinus carpio) are essential components of the pattern ofsarcoplasmic proteins used for fish species identification by isolelectric focusing. In fishery products oflowpH, like marinated herring (pH ∼ 4), parvalbumins were not detectable. It was demonstrated for herring and carp that parvalbumins were not precipitated at pH 4, but were degraded by fish muscle proteases .