文献类型：期刊文献

中文题名：硫酸葡聚糖对低离子强度下罗非鱼肌球蛋白热变性聚集的抑制及其机制

英文题名：Inhibition of heat-induced aggregation of Tilapia myosin by dextran sulfate at low ionic strength

作者：李婷[1,2];周春霞[1,2];冯瑞[1,2];洪鹏志[1,2]

机构：[1]广东海洋大学食品科技学院,广东湛江524088;[2]广东省水产品加工与安全重点实验室,广东湛江524088

年份：2018

卷号：34

期号：12

起止页码：5

中文期刊名：食品与机械

外文期刊名：Food and Machinery

收录：CSTPCD、、北大核心2017、CSCD2017_2018、北大核心、CSCD

基金：广东海洋大学创新强校工程项目(编号:GDOU2013050204);湛江市海洋经济创新发展示范市建设项目(编号:湛海创2017C8B1)

语种：中文

中文关键词：肌球蛋白;低离子强度;热变性聚集;硫酸葡聚糖;抑制机理

外文关键词：myosin;low ionic strength;thermal denatured aggregation;dextran sulfate (DS);inhibition mechanism

中文摘要：以罗非鱼背部白肉为原料提取肌球蛋白,分析在低离子强度(1,50,150 mmol/L KCl)下,硫酸葡聚糖(dextran sulfate,DS)的添加对热处理(40～80℃,1℃/min)过程中肌球蛋白(2.0mg/mL)溶解度和分子结构的影响,探讨DS对肌球蛋白热变性聚集的抑制效果及机理。结果表明,在1mmol/L KCl条件下,肌球蛋白溶解度极低,热处理后分子头部聚集,尾部交联;在50,150mmol/L KCl条件下,肌球蛋白纤丝逐渐解离变粗,热处理后丝状体消失,头部聚集,溶解度、α-螺旋含量明显下降。添加0.4mg/mL DS后,热处理过程中体系浊度、溶解度和α-螺旋含量无明显变化,与未添加DS的体系相比,相同温度条件下肌球蛋白的溶解度明显增大(P<0.05),表面电势升高。DS与肌球蛋白分子间强的静电相互作用能有效抑制低离子强度下肌球蛋白的热变性聚集。

外文摘要：Studied,the inhibitory effect of DS on thermal aggregation of tilapia myosin(2.0 mg/mL)in low ionic strength(1,50,150mmol/L KCl)during the heat treatment(40 ~ 80 ℃,1℃/min).The result showed that the myosin had poor solubility in1mmol/L KCl.While,with the icreased of ionic strengths,myosin fibrils could dissociate in 50 and 150mmol/L KCl.After heating,the myosin filaments disappeared,and the heads and tails of myosin aggregated seriously,resulting in the solubility and the content ofα-helix decreased significantly.After adding 0.4mg/mL DS,the change of turbidity,solubility andα-helix content was not obvious in the range of 40~80℃.Compared to the samples without DS,the solubility,ζ-potential were higher at the same temperature(P<0.05).The results suggested that the strong electrostatic interaction between DS and myosin can effectively inhibit the thermal denaturation of myosin under low ionic strength.