Insight into the Mechanism of Reduced IgG/IgE Binding Capacity in Ovalbumin as Induced by Glycation with Monose Epimers through Liquid Chromatography and High-Resolution Mass Spectrometry

Insight into the Mechanism of Reduced IgG/IgE Binding Capacity in Ovalbumin as Induced by Glycation with Monose Epimers through Liquid Chromatography and High-Resolution Mass Spectrometry
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通过液相色谱和高分辨率质谱深入了解单糖差向异构体糖化引起的卵清蛋白中 IgG/IgE 结合能力降低的机制

DOI:
10.1021/acs.jafc.0c01233
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发表时间:
2020
影响因子:
6.1
通讯作者:
Zhang Jingjing
Zhang Jingjing
中科院分区:
农林科学1区
文献类型:
--
作者:
Yang Yipeng;Liu Guangxian;Tu Zongcai;Wang Hui;Hu Yueming;Mao Jihua;Zhang Jingjing

文献摘要

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卵清蛋白(OVA)是鸡蛋中的主要食物过敏原之一。本研究表明,糖基化与葡萄糖及其外显体(包括d-甘露糖、d-醛糖、d-半乳糖和l-idose)可以有效地减弱OVA的IgG/IgE结合,这是由于糖的共价掩蔽及其结构变化。确定了糖基化位点,并使用液相色谱和高分辨率质谱法找到了它们的平均取代度。用常规光谱法监测OVA构象的波动。与OVA-Man和OVA-Glu相比,OVA-All、OVA-Gal和OVA-Ido的糖基化程度更高,其空间布局变化更为剧烈,说明糖中C-3、C-4和C-5位羟基的构型可能对糖基化反应性有重要影响;因此,它们与IgG/IgE的结合能力下降更为明显。试图提供有价值的信息,以深入了解不同的外聚体糖的生化功能的差异。这些见解将有助于设计具有理想安全水平的甜食品。
Ovalbumin (OVA) is one of the major food allergens in hen eggs. In this work, it was demonstrated that glycation withd-glucose and its epimers, includingd-mannose,d-allose,d-galactose, andl-idose, could effectively attenuate the IgG/IgE binding of OVA, which was attributed to the covalent masking by sugars and to its structural changes. The glycation sites were determined, and their average degree of substitution was found using liquid chromatography coupled with high-resolution mass spectrometry. Fluctuations in OVA conformation were monitored by conventional spectrometry. Compared to those of OVA-Man and OVA-Glu, OVA-All, OVA-Gal, and OVA-Ido showed a higher glycation extent, and the alterations on their steric layouts were more drastic, suggesting that the configuration of hydroxyl groups at positions C-3, C-4, and C-5 in sugars might be important for the glycation reactivity; as such, their capabilities in binding with IgG/IgE decreased more significantly. Attempts were made to provide valuable information for in-depth understanding of the differences in biochemical functionality among epimeric sugars. These insights would be helpful for designing sweetened food products with a desirable level of safety.