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Abstract：
Ovalbumin (OVA) is one of the major food allergens in hen eggs. In this work, it was demonstrated that glycation with d-glucose and its epimers, including d-mannose, d-allose, d-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-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.
摘要：
卵清蛋白(OVA)是鸡蛋中主要的食物过敏原之一。在这项工作中,研究表明，用d-葡萄糖及其差向异构体进行糖基化，包括d-甘露糖,d-合金,D-半乳糖,和l-idose，能有效减弱OVA的IgG/IgE结合，这归因于糖的共价掩蔽及其结构变化。确定糖化位点，和它们的平均取代度是使用液相色谱和高分辨率质谱法发现的。通过常规光谱法监测OVA构象的波动。与OVA-Man和OVA-Glu相比，OVA-All,OVA-Gal,OVA-Ido显示更高的糖基化程度，它们的立体布局的变化更剧烈，表明糖中C-3，C-4和C-5位羟基的构型可能对糖基化反应性很重要；因此，它们与IgG/IgE的结合能力下降更显著.尝试提供有价值的信息，以深入了解差向异构糖之间的生化功能差异。这些见解将有助于设计具有理想安全水平的甜味食品。
