プロパナールおよびカプロン酸による不溶化たん白質の性状 (-20℃貯蔵中の魚肉アクトミオシンの不溶化-1,2-)

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Properties of insolubilized protein formed by the reaction of lipid oxidation products such as propanal or caproic acid with rainbow trout actomyosin during storage at -20°C were studied in KCl-phosphate buffer (I=0.5, pH7.2).These insolubilized proteins retained nearly the same amino acid compositions, but tended to be harder, more elastic and more digestible. In addition, the net-work grade in electron photomicrographs became slender and close. These effects were stronger in the caproic acid addition system than in the propanal addition system. It was considered that the differences in those effects were due to the various progressive degrees of the intra- and/or intermolecular reactions of the proteins, and that these reaction degrees were attributable to propanal and caproic acid having different interaction mechanisms.
日本水産學會の論文