Investigation of the Mechanism of Co-60 Gamma-Ray Irradiation-Stimulated Oxidation Enhancing the Antigenicity of Ovalbumin by High-Resolution Mass Spectrometry
文献类型： 外文期刊
作者： Bian, Zhong-yue 1 ; Tu, Zong-cai 1 ; Wang, Hui 1 ; Hu, Yue-ming 1 ; Liu, Guang-xian 2 ;
作者机构： 1.Nanchang Univ, State Key Lab Food Sci & Technol, Nanchang 330047, Jiangxi, Peoples R China
2.Jiangxi Acad Agr Sci, Inst Food Sci & Technol, Nanchang 330299, Jiangxi, Peoples R China
3.Jiangxi Normal Univ, Natl R&D Ctr Freshwater Fish Proc, Nanchang 330022, Jiangxi, Peoples R China
4.Jiangxi Normal Univ, Engn Res Ctr Freshwater Fish High value Utilizat J, Nanchang 330022, Jiangxi, Peoples R China
关键词： ovalbumin; irradiation; IgG/IgE binding ability; oxidation sites
期刊名称：JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY （ 影响因子：5.895； 五年影响因子：6.048 ）
ISSN： 0021-8561
年卷期：
页码：
收录情况： SCI
摘要： Co-60 gamma-ray irradiation-induced antigenicity changes in ovalbumin (OVA) were investigated, and the molecular mechanism was analyzed. Irradiation treatment at 0-100 kGy could significantly enhance the IgG/IgE binding ability of OVA in a dose-dependent paradigm by concomitant oxidative modification, which exhibited color browning and an increase in carbonyl content caused by high-penetrable rays. More allergenic epitopes of OVA were exposed after irradiation treatment reflected by structural changes including the unfolding of tertiary structure, the conversion of alpha-helix structures to beta-sheet and random coil structures, and the cleavage of several peptide bonds. Meanwhile, three oxidation sites of K46, T49, and N260 located in key linear epitopes were observed, which might increase the allergenic ability of OVA via the disaggregation of noncovalent bonds and the unwinding of alpha-helix structures. Conclusively, irradiation may enhance the potential allergenicity of OVA by oxidative modification, which provides theoretical guidance for effectively controlling the oxidation of proteins in the irradiation process.
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