多獲性多脂魚タンパク質の高度利用-II : マイワシ・サクシニル化筋原繊維タンパク質の化学的性質と機能特性

概要

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The sardine myofibrillar protein was succinylated by reacting with succinic anhydride; the degree of succinylation of this protein was 92%. The chemical and functional properties of the modified proteins were as follows: no specific Ca2+ ATPase activity was observed and the streaming birefringence was negative; the lipid content was reduced to 14% from 33% for the original myofibrillar protein; the water-soluble property was not affected by changes in NaCl concentration; the isoelectric point was around pH 3; the protein in aqueous solution was neither precipitated nor coagulated during heating at 100°C for 10 min; the rheological behavior in the relation of shear stress and rate of shear showed shear-thinning, which is characteristic of a pseudoplastic fluid; and the apparent viscosity tended to become low with the increase of protein concentration. These functional properties appear to make succinylated protein potentially useful as an ingredient in our food system.