Binding of beta-lactoglobulin to three phenolics improves the stability of phenolics studied by multispectral analysis and molecular modeling
文献类型： 外文期刊
作者： Zhang, Shanying 1 ; Li, Xiaolei 1 ; Ai, Binling 1 ; Zheng, Lili 1 ; Zheng, Xiaoyan 1 ; Yang, Yang 1 ; Xiao, Dao 1 ; Sheng, Zhanwu 1 ;
作者机构： 1.Chinese Acad Trop Agr Sci, Haikou Expt Stn, Haikou 570101, Hainan, Peoples R China
2.Hainan Univ, Coll Food Sci & Engn, Haikou 570228, Hainan, Peoples R China
3.Haikou Key Lab Banana Biol, Haikou 571101, Hainan, Peoples R China
关键词： beta-Lactoglobulin; Phenolics; Stability; Interaction mechanism; Muti-spectroscopy; Advanced glycation end product
期刊名称：FOOD CHEMISTRY-X （ 影响因子：6.443； 五年影响因子：6.443 ）
ISSN： 2590-1575
年卷期： 2022 年 15 卷
页码：
收录情况： SCI
摘要： 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 beta-lactoglobulin (beta-LG) and their interaction mechanism was investigated. Fluorescence experiments demonstrated that FA and QT displayed typical static quenching, while VA caused fluorescence sensitization of beta-LG. Furthermore, phenolics changed the secondary structure of beta-LG by inducing the transformation from alpha-helices to beta-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 beta-LG. Furthermore, QT, FA and VA demonstrated good AGEs inhibitory abilities in BSA-fructose, BSA-MGO, arginine-MGO models. These results reveal that beta-LG embedding effectively improves the thermostability and photostability of dietary phenolics in food.
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