宰后成熟期间结构蛋白对秦川牛肉嫩度的影响  

Effect of Structural Protein on Tenderness of Beef from Qinchuan Cattle during Postmortem Aging

作　　者：马旭华 杨波[1] 李亚蕾[1] 罗瑞明[1] 张杏亚 张萌[1] MA Xuhua;YANG Bo;LI Yalei;LUO Ruiming;ZHANG Xingya;ZHANG Meng(School of Food and Wine,Ningxia University,Yinchuan 750021,China)

机构地区：[1]宁夏大学食品与葡萄酒学院,宁夏银川750021

出　　处：《食品科学》2022年第17期199-207,共9页Food Science

基　　金：国家自然科学基金地区科学基金项目(32160535);宁夏回族自治区重点研发项目(2017BY068)。

摘　　要：为探究宰后成熟期间结构蛋白对秦川牛背最长肌嫩度的影响,测定不同贮藏期(0、2、4、6、8 d)内秦川牛背最长肌剪切力、肌原纤维小片化指数(myofibrillar fragmentation index,MFI)和蛋白含量等,并利用4D-非标记定量(4D-label free quantification,4D-LFQ)蛋白质组学技术分析蛋白质组学变化。结果表明:在贮藏期0~8 d内,剪切力总体呈先升后降的趋势(P<0.01),上升的幅度小于下降的幅度;秦川牛背最长肌MFI呈极显著上升趋势(P<0.01),总体增长了250.81%;总可溶性蛋白含量呈显著下降趋势(P<0.05),总体下降了34.60%;通过宰后肌肉组织代谢变化,肌肉组织结构蛋白发生降解,可能会影响到嫩度的形成,肌原纤维蛋白含量呈显著下降趋势(P<0.05),前期下降速度较快,后期下降速度减缓,总体下降了50.56%。在贮藏期0~4 d内,通过骨骼肌组织发育过程调控钙离子结合和细胞骨架蛋白结合途径,4种蛋白(α-肌动蛋白-1、牛肌球蛋白重链9、牛肌球蛋白轻链2、肌球蛋白调节轻链12B)丰富度发生变化;在贮藏期0~8 d内,通过肌肉器官发育和横纹肌组织发育过程调控钙离子结合途径,8种蛋白(肌球蛋白调节轻链2、肌球蛋白重链6、α-肌动蛋白-1、心肌肌动蛋白α1、牛肌球蛋白轻链2、肌钙蛋白I 1型、肌钙蛋白I 2型、肌球蛋白重链15)丰富度发生变化,通过肌球蛋白结合、钙离子结合、细胞骨架蛋白结合的肌原纤维组装、骨骼肌组织发育、肌肉器官发育、横纹肌组织发育过程等途径调控细胞的生理状态,结构蛋白降解造成肌原纤维小片化升高,进而促使嫩度提升。In order to explore the effects of structural proteins on the quality changes of Longissimus dorsi muscle from Qinchuan cattle during storage,4D-label free quantification(4D-LFQ)was used to analyze the proteomic changes of beef Longissimus dorsi muscle during different storage periods(0,2,4,6 and 8 days).The changes in shear force,myofibrillar fragmentation index(MFI)and protein content were measured as well.The results showed that the shear force tended to increase and then decrease during the storage period of 8 days(P<0.01),the increase being greater than the decrease.The MFI showed a significant upward trend with storage time(P<0.01),increasing by up to 250.81%after 8 days of storage;however,the opposite trend was observed for the total soluble protein content(P<0.05),decreasing by up to 34.60%.Structural proteins in muscle tissue were degraded with postmortem metabolic changes in muscle tissue,which possibly affected tenderness development and caused a significant decrease in the content of myofibrillar protein(P<0.05).The content of myofibrillar protein decreased rapidly at first and then slowly,decreasing by 50.56%over the entire storage period.During the first four days,the abundance of four proteins(alpha-actin-1,myosin heavy chain 9,myosin regulatory light chain 2,and myosin regulatory light chain 12B)were changed by regulating the calcium ion-binding and cytoskeletal protein-binding pathways in the development of skeletal muscle tissue.During the 8 days of storage,the abundance of eight proteins(myosin regulatory light chain 2,myosin heavy chain 6,alpha-actin-1,actin,alpha cardiac muscle 1,myosin regulatory light chain 2,troponin I 1,troponin I 2,and myosin heavy chain 15)was changed by regulating the calcium ionbinding pathway in the development of muscle organ and striated muscle tissue.Moreover,the structural proteins were degraded as a result of the regulation of the physiological state of cells by myosin binding,calcium ion binding,cytoskeletal protein binding myofibrillar assembly,skeletal muscle

关 键 词：秦川牛背最长肌 4D-非标蛋白质组学 嫩化机制 结构蛋白 肌原纤维小片化 

分 类 号：TS251.1[轻工技术与工程—农产品加工及贮藏工程]