魚肉たん白質のゲルろ過-IV : 凍結貯蔵肉における溶出性たん白質組成の変化
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In the previous paper, it was reported that the elution patterns by gel filtration of fresh fish muscle protein extracts showed peaks of actomyosin and myogen and that of fresh rabbit muscle protein extract showed peaks of myosin and myogen, and that these elution patterns may provide useful information on the composition of each of the proteins. This paper deals with our attempt in gel filtration to follow the development of denaturation or insolubilization of muscle protein during cold storage. Samples used were muscles of yellowtail (“buri”), Seriola quinqueradiata, sea bass (“suzuki”), Lateolabrax japonicus, and rabbit, and these muscles were stored at -20°C for up to five months. The muscle protein extracts with KCI-phosphate buffer (I=0.5, pH 7.2) were subjected to gel filtration on a Sepharose 2 B column. The elution patterns obtained by gel filtration of fish muscle protein extracts showed peaks of actomyosin (P1) and myogen (P3). During the cold storage, the size of peak P1 decreased steadily, but that of P3 showed no changes (Figs. 1 and 3). For rabbit muscle, however, the elution pattern of protein extract of unfrozen muscle showed peaks of myosin (P2) and myogen (P3), and that of frozen-stored muscle showed P1 and P3. During the cold storage, decrease in the size of P1 was observed, but no changes in that of P3 was observed (Fig. 4). Ultracentrifugal sedimentation patterns of these protein extracts revealed the trend similar to the above-mentioned results obtained by gel filtration (Figs. 2 and 5). The amounts of eluted actomyosin by gel filtration indicated sharper decrease during cold storage than that of extractable myofibrillar proteins fractionated by a usual dilution-precipitation method (I = 0.05) (Tables 1 and 2). These results indicate that actomyosin in muscle protein extracts is a protein which is insolubilized during frozen-storage.
- 公益社団法人 日本水産学会の論文
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