ニジマスアクトミオシン区たん白質とプロパナールおよびカプロン酸の反応機構 (-20℃貯蔵中の魚肉アクトミオシンの不溶化-1,2-)

概要

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The interaction mechanism of lipid oxidation products, such as propanal or caproic acid, with rainbow trout actomyosin (AM) was studied in KCl-phosphate buffer (I=0.5, pH7.2) during storage at -20°C.From the results obtained in the present and the previous studies, the mechanism was hypothesized to be as follows:During storage, AM aggregation and consequent insolubilization occurs, mainly due to intra and intermolecular S-S bonding.Propanal forms mercaptal by reacting with SH groups which appear on the unfolding AM molecule during the initial stage of frozen storage, and thereby accelerates the AM insolubilization.Caproic acid, bound to AM with hydrogen and/or hydrophobic bonds, unbalances the net-charge of the AM molecule thus inducing the insolubilization of the protein.
日本水産學會の論文