乾燥による魚肉蛋白質の変性について

概要

論文の詳細を見る
Denaturation of muscle proteins during dehydration process of flatfish and squid was studied by following the change of solubility. In the course of dehydration, pieces of muscles were taken at intervals, extracted, and the salt-extractable proteins (L), the myosins (M), the non-myosins (N=L-M ), and the waterextractable proteins (S) were determined (Figs. 1 ?? 10). Both in muscles of flatfish and of squid, the salt-extractable proteins and the myosins decreased in parallel to the dehydration (Figs, 3 and 7), but the non-myosins kept a constant level throughout the procedure (Figs. 4 and 8). The amount of the water-extractable proteins of flatfish showed no change on dehydration, being almost equal to the non-myosins (Fig. 4). In the case of squid, however the water-extractable proteins which originally amounted to 50% of total proteins, suddenly dropped down to 6 ?? 9%, when some 40% of moisture was removed from the muscle (Fig. 9). The streaming birefringence which was found in the salt-extracts of flatfish and squid, and in the aqueous extracts of squid, failed to be detected in those of dried muscles, by the apparatus used here, while it was observed in the control groups. It seems most probable that, on dehydration of muscle of flatfish or squid, the myosins are readily denatured, while albumins remain native.
公益社団法人日本水産学会の論文