摘要
通过对鲫肌原纤维蛋白加热过程中浊度、粘度、Ca2+-ATPase活性以及总巯基含量的测定,结合SDS一聚丙烯酰胺凝胶电泳分析了鲫肌原纤维蛋白在加热过程中理化特性的变化。结果表明:鲫肌原纤维蛋白在加热过程中浊度随着溶液温度的升高而上升,在36℃、42℃和48℃条件下变化显著;粘度在20～47℃期间下降,在35℃和47℃出现显著的变化。Ca2+-ATPase活性28～40℃间显著下降,并且在36℃条件下变化显著。总巯基含量结合SDS-PAGE电泳显示,当溶液温度在40℃以上时,蛋白质分子间通过二硫键产生了肌球蛋白重链聚合物以及其它大分子物质。
The changes in physiochemical properties of myofibrillar protein from crucian carp during heat-treatment were studied through the tests of turbidity,viscosity,Ca2＋-ATPase activity,total sulfhydryl content and a SDS-PAGE study.Research on changes in physicochemical properties of myofibrillar protein during heat-treatment can help to understand the thermal denaturation of it and provide practical information for crucian carp muscle processing,so as to promote the utilization of huge amount of freshwater fish resources in China.The results showed that turbidity increased as temperature rose.Turbidity did not show a significant increase from 20 to 34 ℃.With increasing temperature from 36 to 70 ℃,turbidity increased significantly and three peaks of change rate was observed at 36,42 and 48 ℃.No significant shifts were detected when the temperature became above 70 ℃; Viscosity declined from 20 to 47 ℃,and two peaks of change rate were observed at 35 and 47 ℃.No significant shifts were detected when the temperature became above 47 ℃.Ca2＋-ATPase activity decreased from 28 to 40 ℃,at the first stage（ 28-34 ℃） ,Ca2 ＋-ATPase activity decreased slowly,then,from 34 to 40 ℃,Ca2＋-ATPase activity decreased significantly and one peak of change rate was observed at 36 ℃.At 40 ℃ Ca2＋-ATPase activity reduced to zero.Sulphydryl content decreased in ranges 20 to 28 ℃ and 40 to 68 ℃ and kept a certain value at 68 ℃ with a slight increase from 28 to 40 ℃.Electrophoretic analysis indicated high temperature（ ≥40 ℃） induced disulfide bonding between myosin chains and other proteins and formed macromolecular substances.
出处
《水产学报》
CAS
CSCD
北大核心
2010年第8期1303-1308,共6页
Journal of Fisheries of China
基金
现代农业产业技术体系建设专项资金资助(nycytx-49)
国家自然科学基金项目(30871946)
