罗非鱼冷藏期间内源蛋白酶和热休克蛋白70对肌原纤维解离的影响  

Effect of endogenous proteases and heat shock protein 70 on myofibril dissociation during refrigeration in tilapia

作　　者：范铭良 郝淑贤[2] 李来好[2] 陈胜军[2,3] 岑剑伟 吴燕燕[2] 魏涯[2] 相欢[2] 黄卉 FAN Mingliang;HAO Shuxian;LI Laihao;CHEN Shengjun;CEN Jianwei;WU Yanyan;WEI Ya;XIANG Huan;HUANG Hui(College of Food Science,Shanghai Ocean University,Shanghai 201306,China;South China Sea Fisheries Research Institute,China Academy of Fisheries Science,National Aquatic Products Processing Technology R&D Centre,Key Laboratory of Aquatic Products Processing,Ministry of Agriculture and Rural Affairs,Guangzhou 510300,China;Key Laboratory of Efficient Utilization and Processing of Marine Fishery Resources of Hainan Province,Sanya Tropical Fisheries Research Institute,Sanya 572018,China)

机构地区：[1]上海海洋大学食品学院,上海201306 [2]中国水产科学研究院南海水产研究所国家水产品加工技术研发中心农业农村部水产品加工重点实验室,广东广州510300 [3]三亚热带水产研究院海南省深远海渔业资源高效利用与加工重点实验室,海南三亚572018

出　　处：《食品与发酵工业》2023年第11期140-146,共7页Food and Fermentation Industries

基　　金：国家特色淡水鱼产业技术体系项目(CARS-46);“扬帆计划”引进创新创业团队专项资助项目(2015YT02H109);中国水产科学研究院基本科研业务费专项资金项目(2020TD69);中国水产科学研究院南海水产研究所中央级公益性科研院所基本科研业务费专项资金资助项目(2021SD06)。

摘　　要：为研究罗非鱼冷藏期间内源蛋白酶和热休克蛋白70与肌原纤维解离的关系,实验测定了罗非鱼肉在4℃真空包装冷藏48 h内肌原纤维小片化指数、肌原纤维解离、内源蛋白酶活性和热休克蛋白70含量的变化,并对其进行相关性分析。结果表明鱼肉冷藏期间肌原纤维小片化指数变化整体呈增加的趋势,最终为初始值的3.52倍;解离的肌球蛋白重链和肌动蛋白的含量呈升高的趋势,最终分别较初始值提高了70%和65%;pH变化为先减少后略微回升,变化范围为6.5~7.0;组织蛋白酶B、L活性持续增加,组织蛋白酶D和钙激活蛋白酶活性呈先增加后减少的趋势,且分别在8、12 h到达最大值;热休克蛋白70含量为先增加后减少,在4 h时达到最大值,最终相比初始值下降了22.27%;肌原纤维小片化指数与组织蛋白酶B、L活性呈极显著正相关(P<0.01),与肌原纤维解离的肌球蛋白重链和肌动蛋白含量均呈极显著正相关(P<0.01),与热休克蛋白70含量呈显著负相关(P<0.05);热休克蛋白70含量与与组织蛋白酶L呈显著负相关(P<0.05)。组织蛋白酶B、L是影响肌原纤维完整性的关键蛋白酶,热休克蛋白70能与肌原纤维粗丝和细丝结合稳定肌原纤维结构,且组织蛋白酶L可能通过降解热休克蛋白70来影响肌原纤维粗丝和细丝的解离。In order to investigate the relationship between endogenous proteases and heat shock protein 70(HSP 70)with myofibrillar dissociation of tilapia during refrigeration,experiments were performed to determine the changes in myofibril fragmentation index,myofibrillar dissociation,endogenous protease activity,and HSP 70 content of tilapia meat during vacuum-packed refrigeration at 4℃for 48 h,and the correlation analysis was performed.Results showed that an overall increasing trend in the change of myofibril fragmentation index during the refrigeration of fish,ending at 3.52 times the initial value.The dissociated myosin heavy chain and actin content showed an increasing trend,eventually increasing by 70%and 65%respectively from the initial values.The pH were decreasing followed by a slight recovery with a range of 6.5 to 7.0.The activities of cathepsin B and L showed a constant increase,and the activities of cathepsin D and calpain showed a trend of increasing and then decreasing,and reached the maximum at 8 and 12 h,respectively.HSP 70 content showed an increase followed by a decrease,reaching a maximum at 4 h and finally decreasing by 22.27%compared to the initial value.Myofibril fragmentation index showed a highly significant positive correlation with cathepsin B and L activities(P<0.01),and with myofibrillar dissociation of both myosin heavy chain and actin content were highly significantly positively correlated(P<0.01)and negatively correlated with HSP 70 content(P<0.05).HSP 70 can stabilize myofibril structure by binding to thick and thin filaments of myofibrils.HSP 70 content was significantly negatively correlated with cathepsin L(P<0.05).Cathepsin B and L are essential proteases affecting the integrity of myofibrillar,and cathepsin L may affect the dissociation of thick and thin filaments of myogenic fibers by degrading HSP 70.

关 键 词：罗非鱼 内源蛋白酶活性 热休克蛋白70 肌原纤维小片化指数 

分 类 号：TS254.1[轻工技术与工程—水产品加工及贮藏工程]