魚類筋原繊維タンパク質の高温加熱処理による分解

概要

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Isolated carp myofibrils, actin, and myosin were heated at high temperatures, and the products after heating were analyzed with SDS-polyacrylamide gel electrophoresis and gel filtration. When myosin was heated at 100°C or 120°C, myosin heavy chain was degraded to many fragments having different molecular weights. The amount of smaller fragments increased with an increase of heating time. Heated for 60min at 120°C, myosin heavy chain band on the electrophoretogram disappeared, but myosin light chains still remained. The intensity of actin band decreased while heating at 100°C and concurrently new protein bands having lower and higher molecular weights appeared. Heating of actin at 120°C accelerated these changes. The electrophoretic patterns of the proteins solubilized from heat-sterilized fish sausage and canned fish with urea-SDS-2-mercaptoethanol solution were similar to that of the heated myosin.
日本水産學會の論文