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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

文献类型： 外文期刊

作者： Yang, Yipeng 1 ; Liu, Guangxian 3 ; Tu, Zongcai 1 ; Wang, Hui 1 ; Hu, Yueming 1 ; Mao, Jihua 1 ; Zhang, Jingjing 1 ;

作者机构： 1.Nanchang Univ, State Key Lab Food Sci & Technol, Nanchang 330047, Jiangxi, Peoples R China

2.Jiangxi Normal Univ, Coll Life Sci, Engn Res Ctr Freshwater Fish High Value Utilizat, Nanchang 330022, Jiangxi, Peoples R China

3.Jiangxi Acad Agr Sci, Nanchang 330200, Jiangxi, Peoples R China

关键词： OVA; mild condition; glycation; HRLC-MS; epimer

期刊名称：JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY （ 影响因子：5.279； 五年影响因子：5.269 ）

ISSN： 0021-8561

年卷期： 2020 年 68 卷 22 期

页码：

收录情况： SCI

摘要： Ovalbumin (OVA) is one of the major food allergens in hen eggs. In this work, it was demonstrated that glycation with 6-glucose and its epimers, including D-mannose, D-allose, 6-galactose, and L-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-S 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.

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