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

Shanying Zhang; Xiaolei Li; Binling Ai; Lili Zheng; Xiaoyan Zheng; Yang Yang; Dao Xiao; Zhanwu Sheng

doi:10.1016/j.fochx.2022.100369

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

Food Chem X. 2022 Jun 15:15:100369. doi: 10.1016/j.fochx.2022.100369. eCollection 2022 Oct 30.

Authors

Shanying Zhang^{1

2}, Xiaolei Li^{1

2}, Binling Ai^{1

3}, Lili Zheng^{1

3}, Xiaoyan Zheng^{1

3}, Yang Yang^{1

3}, Dao Xiao^{1

3}, Zhanwu Sheng^{1

3}

Affiliations

¹ Haikou Experimental Station, Chinese Academy of Tropical Agricultural Sciences, Haikou 570101, China.
² College of Food Science and Engineering, Hainan University, Haikou 570228, China.
³ Haikou Key Laboratory of Banana Biology, Haikou 571101, China.

Abstract

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.

Keywords: Advanced glycation end product; Interaction mechanism; Muti-spectroscopy; Phenolics; Stability; β-Lactoglobulin.