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

• DOI: 10.1016/j.fochx.2022.100369
• Publication Date: 2022-06-15T12:51:36Z
• Authors: Shanying Zhang; Xiaolei Li; Binling Ai; Lili Zheng; Xiaoyan Zheng; Yang Yang; Dao Xiao; Zhanwu Sheng
• Keywords: 0106 biological sciences; Nutrition. Foods and food supply; TP368-456; β-Lactoglobulin; 01 natural sciences; Food processing and manufacture; Interaction mechanism; TX341-641; Phenolics; Advanced glycation end product; Muti-spectroscopy; Stability; Research Article

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.