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- W1434382020 abstract "This experiment investigated the changes in physiochemical properties of myofibrillar protein from grass carp during heat-treatment so as to expose the law and mechanism of its thermal denaturation. As temperature rose,turbidity of protein solution increased by s-shape curve and climbed quickly at 48 ℃; Viscosity decreased by inverse s-shape curve and greatly declined at 46 ℃; Ca2+-ATPase activity decreased gradually with a slight increase from 36 to 42 ℃ and reduced to blank at 46 ℃; Total sulfhydryl group began to decrease at 40 ℃ and distinctively dropped between range of 60-70 ℃. As heated under stable temperatures (45,55,65 ℃),Ca2+-ATPase activity and viscosity declined while turbidity increased as time prolonged,and the higher temperature is,the changes is more obvious; Total sulfhydryl group decreased distinctively as time prolonged under temperatures higher than 50 ℃. Two enthalpy transitions were found at 46.37 ℃and 62.59 ℃ in DSC graph of myofibrillar protein. SDS-PAGE electrophoresis showed the formation of disulfide group at temperature higher than 45 ℃. Results suggested that myosin suffered conformation changes and aggregation during heating period,leading to the great denaturation of myofibrillar protein." @default.
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- W1434382020 date "2009-01-01" @default.
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- W1434382020 title "Changes in physiochemical properties of grass carp (Ctenopharyngodon idellus) myofibrillar protein during heat-treatment." @default.
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