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

Food Chemistry: X

Lili Zheng¹  Xiaolei Li¹  Dao Xiao²  Yang Yang³  Shanying Zhang⁴  Binling Ai⁴  Xiaoyan Zheng⁴  Zhanwu Sheng⁴ 

[1] College of Food Science and Engineering, Hainan University, Haikou 570228, China;Corresponding authors.;Haikou Key Laboratory of Banana Biology, Haikou 571101, China;Haikou Experimental Station, Chinese Academy of Tropical Agricultural Sciences, Haikou 570101, China;

关键词: β-Lactoglobulin;    Phenolics;    Stability;    Interaction mechanism;    Muti-spectroscopy;    Advanced glycation end product;   

DOI  :  

来源: DOAJ

【 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 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.

【 授权许可】

Unknown