魚類筋形質タンパク質の熱凝固特性
1992 年 58 巻 8 号 p. 1529-1533
詳細
1992 年 58 巻 8 号 p. 1529-1533
To study the mechanism of the gel-strength increasing effect of sarcoplasmic proteins (Sp-P) on fish meat gel, the interaction between each component of Sp-P and actomyosin (AM) occurr-ing during heating was examined. Heat coagulation temperature range was measured for each component by gradually heating the Sp-P extracts (I=0.05) from 9 fish species: 40-50°C for 50K, 43K, and 23K; 50-60°C for 94K, 60K, 40K, 30K, and 25K; 60-70°C for 65K, 63K, 55K, and 35K; >70°C for 20K components>. These components, however, remained in the mixed solution (I=0.7) of Sp-P and AM at a ratio of 1 to 2 even after heating at 80°C. This was attributable to the fact that the coagulable Sp-P components bound to AM molecules one after another at their coagulation temperatures were suspended in the solution.
