コイ筋アクトミオシンの冷凍変性機作の反応速度論的研究〔英文〕

概要

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To assess the mechanism of denaturation of fish muscle proteins during frozen storage, kinetic analysis of the rate of decrease in the solubility of the proteins was undertaken. Actomyosin solution isolated from carp muscle was frozen stored at various conditions of protein concentration, ionic strength, and pH, and the change of protein solubility was studied kinetically. Electron microscopic observations were also carried out to obtain information regarding changes in the shape of the actomyosin filaments. At pH 7.0, no single first order rate was found, but a two staged change consisting of two first order rate processes was illustrated regardless of the protein concentration and ionic strength. However, the mode of change varied depending on the pH. At a pH below 7.0, the change followed two staged process, while, at a pH above 7.5, it occurred in four successive stages, each of which was of a first order expression. From the results, three possible mechanisms have been proposed for the freeze denaturation of actomyosin.
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