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作 者:陈铮[1] 朱蓓薇[1] 李冬梅[1] 姜鹏飞[1] 赵鑫[1] 邓丽[1]
机构地区:[1]大连工业大学食品学院,国家贝类加工技术研究分中心(大连),辽宁大连116034
出 处:《食品与发酵工业》2012年第7期53-57,共5页Food and Fermentation Industries
基 金:国家十二五"863"计划主题项目新型水产品加工装备开发与新技术研究(编号:2011AA100803)
摘 要: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 tem- perature 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 dena- turation 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 ob vious changes were observed at 50 ℃.
分 类 号:TS254.1[轻工技术与工程—水产品加工及贮藏工程]
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