Abstract
When carp muscle slices prepared immediately after slaughter were dipped in 48°C-water for 15 sec and then cooled to 0°C, they were markedly stiffened ang estimated as an excellent “arai”, a Japanese traditional dish. The present study was conducted to reveal the mechanism for such stiffening of muscle. The extent of denaturation of myofibrillar proteins in that “arai” was estimated to be about 40% by measuring EDTA-activated ATPase activity. When a glycerinated fiber, prepared from rabbit psoas muscles, and immersed in relaxing solution was warmed gradually, an abrupt development of 80 mg-isometric tension probably due to the desensitization of regulatory proteins was found at 44°C. That fiber lost the tension by subsequent cooling to 15°C. These reaaults propose the following mechanism: When dipped in 48°C-water, muscles immediately undergo heat contracture followed by heat denaturation, resulting in the stiffening of muscle. In addition, the partial denaturation of actomyosin prevents the stiffened muscles from returning to a relaxing state on cooling. These changes of muscle during the dipping in warmed water give characteristic appearance and taste to the “arai” prepared from fresh carp fillets.
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