各種サメ筋原繊維タンパク質の変性に及ぼす熱,尿素およびpHの促進効果

概要

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The myofibrils from six species of shark were prepared and suspended in a medium of 0.16M KCl-40mM Tris buffer (pH 7.5 or 5.8) containing various concentrations (0-1.0M) of Urea. Thesuspension was then heated at a fixed temperature in the range of 25-45°C and measured for its Ca-ATPase activity with the lapse of time. The first order rate constant for inactivation wasthus calculated. By adopting an increasing ratio of KD as a measure of accelerating effect on denaturation of myofibrillar protein, multiplying effect by the presence of Urea (0.3M), the fall in pH (from 7.5 to 5.8), and the elevation of temperature (from 25°C to 35°C) was observed for all shark myo-fibrils. Among the three factors examined, heat showed the largest effect. From the above data thus obtained, a discussion followed to obtain favourable conditions needed for the preservation and processing of raw muscle from shark.
日本水産學會の論文