Abstract 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.
Journal of Texture Studies – Wiley
Published: Mar 1, 1970
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