Food and Fermentation Industries >

2020 , Vol. 46 >Issue 10: 27 - 34

DOI: https://doi.org/10.13995/j.cnki.11-1802/ts.023743

Effect of hydroxyl radical oxidation on the thermal aggregation behavior of myofibrillar protein from grass carp (Ctenopharyngodonidellus)

  • LI Xuepeng ,
  • LIN Boyan ,
  • WANG Jinxiang ,
  • ZHOU Mingyan ,
  • ZHU Wenhui ,
  • YI Shumin ,
  • LI Jianrong ,
  • LIN Hong ,
  • MOU Weili ,
  • GUO Xiaohua
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  • 1(College of Food Science and Technology, Bohai University, National & Local Joint Engineering Research Center of Storage Processing and Safety Control Technology for Fresh Agricultural Products, National R & D Branch Centre for Surimi and Surimi Products Processing, Jinzhou 121013, China)
    2(College of Food Science and Engineering, the Ocean University of China, Qingdao 266003, China)
    3(Penglai Jinglu Fishery Co., Ltd, Yantai 265600, China)
    4(Shandong Meijia Group Co., Ltd, Rizhao 276815, China)

Received date: 2020-02-24

  Online published: 2020-06-17

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Abstract

Myofibrillar protein from grass carp (Ctenopharyngodonidellus)was first oxidized by different concentrations of hydroxyl radicals (·OH) generated by FeCl3-VC-H2O2 system, and the effect of ·OH oxidation on the thermal aggregation behavior during the heating process was investigated by the measurements of protein thermal stability, surface hydrophobicity, Zeta potential values, endogenous fluorescence, turbidity, particle size and topographical features. The results showed that low-concentration of ·OH oxidation (generated by 0.1-1 mmol/L H2O2) was helpful to improve the thermal stability, while high-concentration of ·OH oxidation (generated by 10 mmol/L H2O2) could reduce the protein thermal stability. The surface hydrophobicity, Zeta potential values, and turbidity of myofibrillar protein in all groups were generally increased first and then decreased with the increase of temperature, while the endogenous fluorescence intensity and the surface hydrophobicity of the 10 mmol/L H2O2treated group decreased. The particle size of control group and the low-concentration of ·OH oxidation groups became larger with the increasing temperature, while the particle size of the 10 mmol/L H2O2treated group decreased after reaching a maximum at 70 ℃. The result of atomic for cemicroscope demonstrated that compared with the non-oxidized group, the aggregated particles formed by the oxidized myofibrillar protein were larger and fewer in number, and the distribution uniformity and shape regularity became worse. The results of this study indicated that low-concentration of ·OH oxidation was beneficial to the thermal aggregation of myofibrillar protein, while high-concentration ·OH oxidation was not favorable to the formation of soluble thermal aggregates. Meanwhile, ·OH oxidation changes the thermal aggregation mode and behavior of myofibrillar protein, which in turn affects the morphological characteristics of its thermal aggregates.

Key words： grass carp; myofibrillar protein; hydroxyl radical; protein oxidation; thermal aggregation

Cite this article

LI Xuepeng , LIN Boyan , WANG Jinxiang , ZHOU Mingyan , ZHU Wenhui , YI Shumin , LI Jianrong , LIN Hong , MOU Weili , GUO Xiaohua . Effect of hydroxyl radical oxidation on the thermal aggregation behavior of myofibrillar protein from grass carp (Ctenopharyngodonidellus)[J]. Food and Fermentation Industries, 2020 , 46(10) : 27 -34 . DOI: 10.13995/j.cnki.11-1802/ts.023743

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