食品科学 ›› 2020, Vol. 41 ›› Issue (5): 1-7.doi: 10.7506/spkx1002-6630-20181231-368

• 基础研究 •    下一篇

基于肌浆蛋白质组研究黑切牛肉的形成机制

吴爽,王磊,杨啸吟,罗欣,李航,朱立贤,张一敏   

  1. (1.山东农业大学食品科学与工程学院,山东 泰安 271018;2.江苏省肉类生产与加工质量安全控制协同创新中心,江苏 南京 210095;3.国家肉牛牦牛产业技术体系丰都综合试验站,重庆 408216)
  • 出版日期:2020-03-15 发布日期:2020-03-23
  • 基金资助:
    国家自然科学基金青年科学基金项目(31601528);现代农业产业技术体系建设专项(CARS-37); 山东省牛产业创新团队项目(SDAIT-09-09)

Understanding the Formation Mechanism of Dark Cutting Beef Based on Sarcoplasmic Proteomics

WU Shuang, WANG Lei, YANG Xiaoyin, LUO Xin, LI Hang, ZHU Lixian, ZHANG Yimin   

  1. (1. College of Food Science and Engineering, Shandong Agricultural University, Tai’an 271018, China; 2. Jiangsu Collaborative Innovation Center of Meat Production and Processing, Quality and Safety Control, Nanjing 210095, China; 3. Fengdu Station of China Agriculture Research System (Beef), Chongqing 408216, China)
  • Online:2020-03-15 Published:2020-03-23

摘要: 本研究通过比较黑切牛肉(黑切组,极限pH 6.54)和正常牛肉(正常组,极限pH 5.59)在宰后45 min和24 h的肌浆蛋白质组,确定黑切牛肉与正常牛肉的差异表达蛋白,从蛋白质水平上探究了黑切牛肉形成的相关机制。结果显示,两个处理组在宰后45 min和24 h共有20 个差异表达蛋白,其中9 个为代谢酶、4 个为抗氧化蛋白、4 个为伴侣蛋白。能量代谢酶类中,仅腺苷酸激酶1的表达量在宰后24 h后的黑切组高于正常组,腺苷酸激酶、肌酸激酶M、磷酸酶、琥珀酸-辅酶A连接酶、磷酸酯尿苷基转移酶和S-腺苷高半胱氨酸均在正常组表达量较高;两种糖酵解酶(肌肉磷酸化酶和葡萄糖磷酸变位酶1)也在正常组中表达量较高;抗氧化蛋白、热休克蛋白B1和B6均在正常组中表达量高,而α-晶状体蛋白则在黑切组中表达量较高。本研究发现,黑切组中一些参与糖代谢和腺嘌呤核苷三磷酸合成和代谢的酶类的低量表达,可能是黑切肉形成的最直接原因。另外,琥珀酸-辅酶A连接酶、热休克蛋白B1和α-晶状体蛋白可以作为识别黑切肉发生的蛋白质生物标签。

关键词: 黑切牛肉, 肌浆蛋白质组, 代谢酶, 抗氧化蛋白, 伴侣蛋白

Abstract: The present study explored the mechanism of the occurrence of dark cutting beef through comparing the sarcoplasmic proteomics of normal pH (5.59) and dark cutting beef (pH 6.54) at 45 min and 24 h post-mortem and analyzing the differentially expressed proteins. The results revealed that 20 differentially expressed proteins were identified. Of these proteins, 9 were metabolic enzymes, 4 were antioxidant proteins and 4 were chaperones. Compared with dark cutting beef, all energy-related enzymes (adenylate kinase 1, creatine kinase M chain, Phospholysine phosphohistidine inorganic pyrophosphate phosphatase, succinate-CoA ligase, UTP-glucose-1-phosphate uridylyltransferase, and S-adenosylhomocysteine hydrolase) except adenylate kinase 1 (which was overexpressed in dark cutting beef) at postmortem 24 h, and the glycometabolic enzymes (phosphoglucomutase 1 and myophosphorylase) were overexpressed in normal pH beef. All antioxidant proteins, and heat shock protein beta-1 and beta-2 were overexpressed in normal pH beef, while alpha-crystallin B chain was overexpressed in dark cutting beef. The development of dark cutting beef could be directly explained by lower abundances of glycometabolic enzymes and energy-related enzymes when compared to normal pH beef. Moreover, succinate-CoA ligase, heat shock protein beta-1 and alpha-crystallin could be employed as biomarkers to identify dark cutting beef.

Key words: dark cutting beef, sarcoplasmic proteomics, metabolic enzymes, antioxidant protein, chaperones

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