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PARAMETERS OF TEXTURE CHANGE IN PROCESSED FISH: MYOSIN DENATURATION
Author(s) -
CHU GEORGE HAO,
STERLING CLARENCE
Publication year - 1970
Publication title -
journal of texture studies
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.593
H-Index - 54
eISSN - 1745-4603
pISSN - 0022-4901
DOI - 10.1111/j.1745-4603.1970.tb00725.x
Subject(s) - denaturation (fissile materials) , myosin , dehydration , isoelectric point , chemistry , texture (cosmology) , solubility , food science , chromatography , viscosity , biophysics , biochemistry , materials science , biology , nuclear chemistry , organic chemistry , composite material , artificial intelligence , computer science , image (mathematics) , enzyme
The white muscle of the Sacramento blackfish ( Orthodon microlepidotus ) was processed by freezing, dehydration, and cooking. Myosin was extracted immediately afterwards or following a period of storage in order to examine evidence for denaturation. The tests used were the solubility of whole muscle protein and the intrinsic viscosity, isoelectric point, ATPase activity, ultra‐violet absorption spectrum, and optical rotatory dispersion of purified myosin extract. Almost all measures used showed that denaturation increased in the order: fresh < frozen < frozen‐stored < dehydrated < dehydrated‐stored < cooked.