Deciphering Changes in the Structure and IgE-Binding Ability of Ovalbumin Glycated by α‑Dicarbonyl Compounds under Simulated Heating

• Published in: Journal of agricultural and food chemistry 2022-02, Vol.70 (6), p.1984-1995
• Main Authors: Zhang, Qiaozhi, Huang, Zhijie, Li, Huatao, Cen, Congnan, Zheng, Ruixing, Lili, Cao, Zhang, Shufen, Wang, Yanbo, Fu, Linglin
• Format: Article
• Language: English
• Subjects: Dietary Proteins - chemistry; Food Safety and Toxicology; Glycation End Products, Advanced; Glyoxal; Hot Temperature; Immunoglobulin E; Ovalbumin - chemistry; Pyruvaldehyde
• ISSN: 0021-8561; 1520-5118
• DOI: 10.1021/acs.jafc.1c06939

As a complex reaction, biological consequences of the Maillard reaction (MR) on dietary proteins need to be deciphered. Despite previous studies on the structural and antigenic properties of ovalbumin (OVA) by MR, associated changes induced by specific MR intermediates and their downstream products are largely unknown. This study focused on the impacts of glycation by α-dicarbonyl compounds (α-DCs), intermediates of MR and precursors of advanced glycation end-products (AGEs), on the structural and IgE-binding properties of ovalbumin (OVA) under simulated heating. Methylglyoxal (MGO), glyoxal (GO), and butanedione (BU) were selected as typical α-DCs to generate glycated OVA with different AGE-modifications (AGE-Ms). The results showed that reactions between OVA and α-DCs generated OVA-AGE with various degrees of modification and conformational unfolding, and the reactivity of α-DCs followed the order GO > MGO > BU. Depending on the precursor type, the levels of 10 specific AGEs were verified, and the amounts of total AGEs increased with heating temperature and α-DC dosage. Compared to native OVA, glycated OVA showed reduced IgE-binding levels but with sRAGE-binding ligands, the extent of which was associated with the contents of total AGEs and Nε-carboxymethyllysine, and changes in certain protein conformational structures. High-resolution mass spectrometry further identified different AGE-Ms on the Lys and Arg residues of OVA, confirming variations in the glycation sites and their associations with the immunoreactive epitopes of OVA under different conditions.