Abstract
This study aimed to investigate the effects of active soybean isoflavones on the structure and potential allergenicity of glycinin, a major allergen, in soybean. The interaction mechanism between two active soybean isoflavones, namely, genistein (Gen) and daidzein (Dai), and glycinin were investigated using a series of spectral techniques. The structure of the isoflavone-glycinin complexes was characterized by SDS-PAGE and spectral techniques. In addition, the potential allergenicity of the isoflavone-glycinin complexes and their digestion products in vitro was measured via Western blot and enzyme-linked immunosorbent assay. Results showed that Gen and Dai effectively quenched the intrinsic fluorescence of glycinin largely through static quenching. Dai interacted with glycinin through hydrogen bonding and van der Waals forces, while Gen relied on hydrophobic interactions with glycinin. Furthermore, the neutral complex of daidzein-glycinin (Dai-G) exhibited weaker IgE binding ability compared with the glycinin samples. These findings provided new insights into the molecular mechanisms that underlay the immunomodulatory effects of soybean isoflavones and their potential applications in food allergy prevention and management.
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