食品科学 ›› 2022, Vol. 43 ›› Issue (17): 199-207.doi: 10.7506/spkx1002-6630-20210706-050

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宰后成熟期间结构蛋白对秦川牛肉嫩度的影响

马旭华,杨波,李亚蕾,罗瑞明,张杏亚,张萌   

  1. (宁夏大学食品与葡萄酒学院,宁夏 银川 750021)
  • 出版日期:2022-09-15 发布日期:2022-09-28
  • 基金资助:
    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)

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

MA Xuhua, YANG Bo, LI Yalei, LUO Ruiming, ZHANG Xingya, ZHANG Meng   

  1. (School of Food and Wine, Ningxia University, Yinchuan 750021, China)
  • Online:2022-09-15 Published:2022-09-28

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。

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

Abstract: 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 ion-binding 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 tissue development, muscle organ development, and striated muscle tissue development, leading to an increase in the MFI, thus improving the tenderness.

Key words: Longissimus dorsi from Qinchuan cattle; 4D-label free quantification; tenderization mechanism; structural proteins; myofibrillar fragmentation

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