李娜, 赵永强, 李来好, 杨贤庆, 郝淑贤, 魏涯, 岑剑伟, 张红杰. 冰藏过程中罗非鱼鱼片肌肉蛋白质变化[J]. 南方水产科学, 2016, 12(2): 88-94. DOI: 10.3969/j.issn.2095-0780.2016.02.013
引用本文: 李娜, 赵永强, 李来好, 杨贤庆, 郝淑贤, 魏涯, 岑剑伟, 张红杰. 冰藏过程中罗非鱼鱼片肌肉蛋白质变化[J]. 南方水产科学, 2016, 12(2): 88-94. DOI: 10.3969/j.issn.2095-0780.2016.02.013
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LI Na, ZHAO Yongqiang, LI Laihao, YANG Xianqing, HAO Shuxian, WEI Ya, CEN Jianwei, ZHANG Hongjie. Change of muscle proteins in Nile tilapia fillets during iced storage[J]. South China Fisheries Science, 2016, 12(2): 88-94. DOI: 10.3969/j.issn.2095-0780.2016.02.013
Citation: LI Na, ZHAO Yongqiang, LI Laihao, YANG Xianqing, HAO Shuxian, WEI Ya, CEN Jianwei, ZHANG Hongjie. Change of muscle proteins in Nile tilapia fillets during iced storage[J]. South China Fisheries Science, 2016, 12(2): 88-94. DOI: 10.3969/j.issn.2095-0780.2016.02.013
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冰藏过程中罗非鱼鱼片肌肉蛋白质变化

Change of muscle proteins in Nile tilapia fillets during iced storage

    摘要
  • 摘要: 为研究冰藏过程中罗非鱼( Oreochromis niloticus) 肌肉蛋白质的变化, 提取了冰藏罗非鱼鱼片肌肉中的不同溶解性蛋白质与不同结构蛋白质, 并分析其在贮藏期间含量的变化, 对总可溶性、水溶性、高盐溶性和低盐溶性蛋白质分别进行十二烷基硫酸钠-聚丙烯酰胺凝胶电泳( SDS-PAGE) , 考察蛋白质的降解情况。结果表明, 冰藏期间高盐溶性蛋白质质量分数由84.99 mgg-1 下降至49.47 mgg-1 , 降低了41.79% ; 水溶性蛋白质质量分数由72.27 mgg-1下降至18.7 mgg-1 , 降低了74.58% ; 低盐溶性蛋白质质量分数分数由11.15 mgg-1 下降至 3. 39 mgg-1 , 降低了69.60% 。3 种不同结构蛋白质中, 肌原纤维蛋白质量分数下降最为明显( 由122. 10 mgg-1 下降至48. 65 mgg- 1 , P 0.05) , 肌浆蛋白质量分数也持续降低( 由37.79 mgg-1 下降至26. 57 mgg-1 , P 0.05) , 肌基质蛋白质量分数无明显变化( P 0.05) 。SDS-PAGE 图谱显示, 肌球蛋白重链、肌动蛋白、原肌球蛋白及其他一些蛋白质条带逐渐减弱, 在贮藏末期还出现了一些新的条带。

     

    Abstract: We extracted different solubility proteins and structure proteins from Nile tilapia ( Oreochromis niloticus) fillets during iced storage to investigate the change of their muscle proteins. The degradation of total soluble, water soluble, high-salt soluble and low-salt soluble proteins was analyzed by SDS-PAGE. The high-salt soluble protein content declined from84. 99 mgg-1 to 49.47 mgg-1 ; water-soluble protein declined from72.27 mgg-1 to 18.37 mgg-1 ; low salt soluble protein dropped from11.15 mgg-1 to 3.39 mgg-1 . In the three different structures of proteins, the decline of myofibrillar protein content is most obvious ( decreased from122.10 mgg-1 to 48.65 mgg-1 , P 0.05) , and the content of myosinogen decreased from37. 79 mgg- 1 to 26.57 mgg- 1 ( P 0.05) , while myostromin had no obvious change ( P 0.05) . The decrease of myosin heavy chain, actin, tropomyosin and some other protein bands in SDS-PAGE patterns indicates degradation of these proteins. Some new bands appeared at the last phase of storage.

     

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