Abstract
Physicochemical changes in bovine natural actomyosin extracted from prerigor semimembranosus muscle were investigated during frozen storage at −28°C as affected by the addition of cryoprotectants (5.6% Polydextrose® or 5.6% mixture (1:1) of sucrose and sorbitol). Proteins were destabilized during freezing and frozen storage as reflected by decreases in protein solubility, the visual appearance of aggregates in protein sols, decrease in intensity of flow birefringence, intrinsic viscosity and ATPase activity, and changes in size, shape, or charge of the protein (especially myosin) as evidenced by nondenaturing electrophoresis. These effects were reduced to some extent by the two cryoprotectant treatments.
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