食品科学 ›› 2019, Vol. 40 ›› Issue (15): 31-36.doi: 10.7506/spkx1002-6630-20180910-097

• 基础研究 • 上一篇    下一篇

羟自由基氧化对高白鲑肌原纤维蛋白降解的影响

秦军委,雷用东,邱恒恒,郭 欣,朱新荣,张 建   

  1. 1.石河子大学食品学院,新疆 石河子 832003;2.新疆农垦科学院,新疆 石河子 832000
  • 出版日期:2019-08-15 发布日期:2019-08-26
  • 基金资助:
    国家自然科学基金地区科学基金项目(31460438);石河子大学重大科技攻关计划项目(gxjs2015-zdgg06);新疆自治区研究生教育创新计划科研创新项目(XJGRI2017038)

Effect of Hydroxyl Radical Oxidation on Degradation of Myofibrillar Proteins from Coregonus peled

QIN Junwei, LEI Yongdong, QIU Hengheng, GUO Xin, ZHU Xinrong, ZHANG Jian   

  1. 1. Food College, Shihezi University, Shihezi 832003, China; 2. Xinjiang Academy of Agriculture and Reclamation Science, Shihezi 832000, China
  • Online:2019-08-15 Published:2019-08-26

摘要: 为了探究羟自由基氧化对鱼肉宰后贮藏期间肌肉蛋白降解的影响,以高白鲑为研究对象,取其背部肌肉进行氧化,研究羟自由基氧化对高白鲑肌原纤维蛋白降解的影响。设置4 组不同浓度的氧化体系(1 mmol/L H2O2+0.2 mmol/L FeCl3、5 mmol/L H2O2+0.4 mmol/L FeCl3、10 mmol/L H2O2+0.8 mmol/L FeCl3、20 mmol/L H2O2+1.0 mmol/L FeCl3),并分别室温氧化0、15、30、60、90 min,以羰基含量确定最适氧化浓度和时间;氧化样品于4 ℃贮藏,分别在0、1、7、14 d取样,通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳和蛋白质免疫印迹检测肌球蛋白重链(myosin heavy chain,MHC)、肌动蛋白、肌间线蛋白和肌钙蛋白T等蛋白的降解程度。结果表明:5 mmol/L H2O2+0.4 mmol/L FeCl3的氧化浓度下孵育60 min为本实验最适氧化条件;氧化组MHC的降解率比未氧化组高,羟自由基氧化显著促进了MHC的降解(P<0.05);肌动蛋白变化不显著(P>0.05),自然降解占主导地位;氧化组中肌间线蛋白和肌钙蛋白T的降解率低于未氧化组,羟自由基氧化抑制了肌间线蛋白和肌钙蛋白T的降解。综上所述,羟自由基氧化主要促进肌纤维中粗丝蛋白的降解,对细丝蛋白的降解没有明显影响,对细胞骨架蛋白和连接蛋白的降解起到抑制作用。

关键词: 高白鲑, 羟自由基, 氧化, 肌原纤维蛋白, 降解

Abstract: The aim of this study was to explore the effect of hydroxyl radical oxidation on the degradation of myofibrillar proteins in the dorsal muscle of Coregonus peled. Four oxidation systems of 1 mmol/L H2O2 + 0.2 mmol/L FeCl3, 5 mmol/L H2O2 + 0.4 mmol/L FeCl3, 10 mmol/L H2O2 + 0.8 mmol/L FeCl3, and 20 mmol/L H2O2 + 1.0 mmol/L FeCl3 were set up, and the oxidation was carried out at ambient temperature for 0, 15, 30, 60 or 90 min, respectively. The optimal oxidation concentration and time were determined based on protein carbonyl content. Then the oxidized fillets were stored at 4 ℃ and sampled after 0, 1, 7, and 14 days to examine the degree of degradation of myosin heavy chain (MHC), actin, desmin and troponin-T of myofibrillar proteins by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Western blotting. The results showed that the optimal oxidation conditions were determined as incubation for 60 min in 5 mmol/L H2O2 + 0.4 mmol/L FeCl3. Compared with native MHC, the degradation of oxidized MHC was enhanced. Hydroxyl radical oxidation remarkably accelerated the degradation of MHC (P < 0.05). There was no significant change in the degradation of actin between the oxidized and non-oxidized groups after the same storage time (P > 0.05), suggesting that the natural degradation of actin was dominant during storage. According to the Western blotting analysis, the degradation efficiencies of both desmin and troponin-T in the oxidized group were lower than in the non-oxidized group, implying that hydroxyl radical oxidation inhibits the degradation of desmin and troponin-T. Overall, our results demonstrate that hydroxyl radical oxidation promotes the degradation of myofibrillar proteins of thick filaments, but has little influence on that of thin filaments and inhibits the degradation of cytoskeletal and junctional proteins.

Key words: Coregonus peled, hydroxyl radical, oxidation, myofibrillar protein, degradation

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