通过对牡蛎闭壳肌肌原纤维蛋白加热过程中浊度、溶解度、表面疏水性、α螺旋含量和总巯基含量的测定,研究了热处理过程中牡蛎闭壳肌肌原纤维蛋白理化特性的变化,结果表明,在20～40℃,牡蛎闭壳肌肌原纤维蛋白溶液的浊度、溶解度、表面疏水性、α螺旋含量和总巯基含量均无明显变化。在温度高于40℃时,随着温度的升高,牡蛎闭壳肌肌原纤维蛋白的浊度整体呈增大趋势,46℃下变化最为明显;溶解度在40～50℃变化最大,结合浊度的变化规律推测其变性温度为46℃;表面疏水性总体上逐渐增加,在40～50℃变化最大;α螺旋含量总体上逐渐降低,60℃变化最大,当温度达到70℃时约有80%的α螺旋结构被破坏;总巯基含量逐渐降低,50℃时下降最快。

The effects of heat treatment on the physiochemical properties changes of myofibrillar proteins from oyster adductor muscle including turbidity,solubility,surface hydrophobicity,α helix content and total sulphydryl content were investigated.The results showed that all the above indicators remained invariable when the heating temperature was 20～40 ℃.When the temperature was higher than 40 ℃,obvious changes of the above indicators were obtained.As the temperature rised,the turbidity of the oyster myofibrillar proteins increased gradually and changed remarkably at 46℃.The solubility and surface hydrophobicity both changed obviously during 40～50℃ and the denaturation temperature was determined to be 46 ℃.The α helix content of myofibrillar protein decreased gradually and the most rapid changes occurred at 60 ℃.About 80% of the α helix was damaged when the temperature increased to 70℃.The total sulphydryl content decreased gradually when the temperature was higher than 40 ℃,and the most obvious changes were observed at 50 ℃.