Insight into the Mechanism Underlying the Reduction of Digestibility and IgG/IgE Binding Ability in Ovalbumin during Different High-Temperature Conduction Modes-Induced Glycation

卵清蛋白 糖基化 免疫球蛋白E 化学 表位 圆二色性 消化(炼金术) 免疫球蛋白G 免疫学 色谱法 生物化学 生物 抗体 受体 抗原
作者
Haiqi Chen,Zongcai Tu,Yanru Zhou,Zuohua Xie,Siqiong Zhang,Pingwei Wen,Jiaojiao Liu,Qiannan Jiang,Hui Wang,Yueming Hu
出处
期刊:Journal of Agricultural and Food Chemistry [American Chemical Society]
卷期号:72 (5): 2801-2812
标识
DOI:10.1021/acs.jafc.3c08882
摘要

Effects of different high-temperature conduction modes [high-temperature air conduction (HAC), high-temperature contact conduction (HCC), high-temperature steam conduction (HSC)]-induced glycation on the digestibility and IgG/IgE-binding ability of ovalbumin (OVA) were studied and the mechanisms were investigated. The conformation in OVA-HSC showed minimal structural changes based on circular dichroism, fluorescence, and ultraviolet spectroscopy. The degree of hydrolysis analysis indicated that glycated OVA was more resistant to digestive enzymes. Liquid chromatography–Orbitrap mass spectrometry identified 11, 14, and 15 glycation sites in OVA-HAC, OVA-HCC, and OVA-HSC, respectively. The IgG/IgE-binding ability of OVA was reduced during glycation and digestion, and the interactions among glycation, allergenicity, and digestibility were further investigated. Glycation sites masked the IgG/IgE epitopes resulting in a reduction in allergenicity. Digestion enzymes destroyed the IgG/IgE epitopes thus reducing allergenicity. Meanwhile, the glycation site in proximity to the digestion site of pepsin was observed to cause a reduction in digestibility.
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