Binding of β-lactoglobulin to three phenolics improves the stability of phenolics studied by multispectral analysis and molecular modeling

• Published in: Food Chemistry: X 2022-10, Vol.15, p.100369-100369, Article 100369
• Main Authors: Zhang, Shanying, Li, Xiaolei, Ai, Binling, Zheng, Lili, Zheng, Xiaoyan, Yang, Yang, Xiao, Dao, Sheng, Zhanwu
• Format: Article
• Language: English
• Subjects: Advanced glycation end product; Interaction mechanism; Muti-spectroscopy; Phenolics; Stability; β-Lactoglobulin
• ISSN: 2590-1575; 2590-1575
• DOI: 10.1016/j.fochx.2022.100369

•Ferulic acid (FA), quercetin (QT), and vanillic acid (VA) can reduce AGEs production.•Phenolics changed the secondary structure of β-lactoglobulin (β-LG).•The binding pattern were explored by molecular docking, molecular dynamic simulation.•β-LG embedding improves the thermostability and photostability of dietary phenolics. Phenolics have been used to suppress the formation of advanced glycation end products (AGEs) in food; however, enhancing their thermostability and photostability in foods remains a key issue. Ferulic acid (FA), quercetin (QT), and vanillic acid (VA), which reduce production of AGEs, were embedded in bovine β-lactoglobulin (β-LG) and their interaction mechanism was investigated. Fluorescence experiments demonstrated that FA and QT displayed typical static quenching, while VA caused fluorescence sensitization of β-LG. Furthermore, phenolics changed the secondary structure of β-LG by inducing the transformation from α-helices to β-structures, with Van der Waals forces and hydrogen bonds as the primary underlying forces. The thermal and photostability of FA/QT/VA was significantly improved upon binding to β-LG. Furthermore, QT, FA and VA demonstrated good AGEs inhibitory abilities in BSA-fructose, BSA-MGO, arginine-MGO models. These results reveal that β-LG embedding effectively improves the thermostability and photostability of dietary phenolics in food.