マイワシ・アセチ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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Sardine myofibrillar protein was acetylated by reacting acetic anhydride at 0°C and pH 8.5. The degree of acetylation of this protein was 92.6%. The acetylated protein showed no specific Ca2+ ATPase activity and little streaming birefringence. Lipid content was slightly reduced to 25.6% from 25.8% of the original myofibrillar protein. The acetylated protein was water soluble at pH 7.0. The solubility was not affected by NaC1 concentration of up to 5%. The isoelectric point was pH 4.0. The protein in aqueous solution was neither precipitated nor coagulated uponheating at 100°C for 10min. The rheological behavior showed shear-thinning at all concentrations of untreated and Triton X-100 treated types of myofibrillar protein and its acetylated protein. However, the acetylated protein showed a Newtonian flow behavior at 0.75%, but tended to exhibit shear-thickening at 0.25%. A shift in molecular weight distribution to lower species occurred when the myofibrillar protein was exhaustively acetylated. Data are also presented on some nutritional properties of the acetylated myofibrillar protein.
公益社団法人日本水産学会の論文