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• 食品化学 •    下一篇

鸡蛋中卵白蛋白和溶菌酶相互作用对其结构和致敏性的影响

汪吴晶1,高金燕2   

  1. 1. 南昌大学国家重点实验室
    2. 南昌大学
  • 收稿日期:2019-01-24 修回日期:2019-11-28 出版日期:2020-03-25 发布日期:2020-03-23
  • 通讯作者: 高金燕 E-mail:gaojy2013@ncu.edu.cn
  • 基金资助:
    国家重点研发计划项目;国家自然科学基金项目

Effects of Interaction on the Structure and Potential allergenicity of Ovalbumin and Lysozyme

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  • Received:2019-01-24 Revised:2019-11-28 Online:2020-03-25 Published:2020-03-23

摘要: 为了了解蛋白质在热处理中相互作用对结构和致敏性的影响,以蛋清中卵白蛋白和溶菌酶为对象,对其在不同温度下的相互作用情况进行了研究,通过浊度、溶解度、SDS-PAGE对其物理性质进行了分析,利用圆二色光谱、紫外光谱、荧光光谱的光谱分析方法对其空间结构进行了表征,并通过竞争ELISA的方法对蛋白质的IgG、IgE结合能力进行了探究。结果表明OVA-Lys在60、65℃下加热10min后不会显著影响彼此的结构以及潜在致敏性,而在70℃下,由于OVA三级结构的展开,Lys疏水基团的暴露,两者会通过二硫键相互作用从而显著降低彼此的潜在致敏性。

关键词: 卵白蛋白, 溶菌酶, 相互作用, 结构, 致敏性

Abstract: To understand the effect of protein-protein interaction on structure and allergenicity during heat treatment, the interaction of ovalbumin (OVA) and lysozyme (Lys) in egg white at different temperatures was studied. The physical properties were analyzed by turbidity, solubility and SDS-PAGE. The spatial structure was characterized by circular dichroism spectroscopy, ultraviolet spectroscopy and fluorescence spectroscopy. The IgG and IgE binding ability were studied by competitive ELISA. The results showed that OVA-Lys interaction after heating for 10 minutes at 60 and 65℃ did not significantly affect the structure and potential allergenicity of each other. However, when treated at 70℃, the tertiary structure of OVA was unfolded, and the hydrophobic groups of Lys were exposed. The interaction between OVA and Lyswas formed through disulfide bonds which could significantly reduce the potential allergenicity of each other.

Key words: ovalbumin, lysozyme, interaction, structure, allergenicity

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