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Low-voltage electrostatic field enhances the frozen force of-12 degree celsius to suppress oxidative denaturation of the lamb protein during the subsequent frozen storage process after finishing initial freezing

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文献类型：外文期刊

作者： Yang, Chuan ¹ ; Wu, Guangyu ¹ ; Liu, Yunhe ¹ ; Li, Yingbiao ³ ; Zhang, Chunhui ¹ ; Liu, Chengjiang ² ; Li, Xia ¹ ;

作者机构： 1.Chinese Acad Agr Sci, Inst Food Sci & Technol, Key Lab Agroprod Proc, Minist Agr & Rural Affairs, Beijing 100193, Peoples R China

2.Xinjiang Acad Agr & Reclamat Sci, Inst Agroprod Proc Sci & Technol, Shihezi 832000, Peoples R China

3.Shihezi Univ, Sch Food Sci & Technol, Key Lab Food Nutr & Safety Control Xinjiang Prod &, Shihezi 832003, Xinjiang, Peoples R China

4.Shihezi Univ, Sch Food Sci & Technol, Key Lab Agr Prod Proc & Qual Control Specialty Coc, Shihezi 832003, Xinjiang, Peoples R China

关键词： Lamb; Low-voltage electrostatic field; Microstructure; Protein oxidative denaturation

期刊名称：FOOD CHEMISTRY （影响因子：8.8；五年影响因子：8.6 ）

ISSN： 0308-8146

年卷期： 2024 年 438 卷

页码：

收录情况： SCI

摘要： The effect of low-voltage electrostatic field (LVEF) assisted -9 degrees C (LVEF-9) and -12 degrees C (LVEF-12) frozen, non-LVEF-assisted -9 degrees C (NLVEF-9) and -12 degrees C (NLVEF-12) frozen, and conventional frozen (CF-18, -18 degrees C) storage on the muscle microstructure and the oxidative denaturation of the lamb protein during the subsequent frozen storage process after finishing initial freezing was investigated. Compared with NLVEF-9, LVEF-9, and NLVEF-12, LVEF-12 maintained the better integrity of muscle microstructure, demonstrated by smaller holes, more complete Z-line and M-line, and no significant difference with CF-18 (P > 0.05). Furthermore, LVEF-12 effectively inhibited protein oxidative denaturation as shown by the lower carbonyl content, surface hydrophobicity, and higher total/active sulfhydryl groups and Ca2+-ATPase activity. Moreover, LVEF-12 effectively maintained the integrity of the secondary and tertiary structure of proteins, reduced cross-linking aggregation of proteins, and sustained better functional properties, as shown by higher alpha-helix content, fluorescence intensity, protein solubility, and lower R-value, disulfide bonds.

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