Effects of ionic strength and (-)-epigallocatechin gallate on physicochemical characteristics of soybean 11S and 7S proteins

文献类型： 外文期刊

第一作者： Yang, Yaxuan

作者： Yang, Yaxuan;Wang, Qiming;Tang, Yuwan;Lei, Lin;Zhao, Jichun;Zhang, Yuhao;Ming, Jian;Li, Lin;Wang, Qiang

作者机构：

关键词： NaCl concentration; Soybean 11S; Soybean 7S; (-)-Epigallocatechin gallate; Physicochemical properties

期刊名称：FOOD HYDROCOLLOIDS （ 影响因子：9.147； 五年影响因子：9.169 ）

ISSN： 0268-005X

年卷期： 2021 年 119 卷

页码：

收录情况： SCI

摘要： Polyphenols can interact with proteins to improve their physicochemical and functional properties. This study was aimed to determine the interactions of EGCG with 11S and 7S at different NaCl concentrations. Results of turbidity indicated that the binding affinity of EGCG with 11S and 7S were strongest at 0.3 M NaCl concentration. Zeta potential results confirmed that 11S-EGCG and 7S-EGCG complexes had stronger stability in salt solutions, but the stability decreased with the increase of NaCl concentration to 0.6 M. Fourier transform infrared spectra showed that NaCl could affect hydrogen bonds between soybean proteins and EGCG. Based on Raman spectroscopy, the microenvironment of the tryptophan and tyrosine residues and intermolecular hydrogen of 11S, 7S, 11S-EGCG and 7S-EGCG were influenced by NaCl concentration. The NaCl induced a decrease in alpha-helix and an increase in beta-sheet of 11S protein, while the secondary structure of 7S was not sensitive to NaCl concentration. The bindings of EGCG to 11S and 7S resulted in the secondary structure rearrangement of two proteins. The NaCl addition led the transformation of the alpha-helix to the beta-sheet in 11S-EGCG and 7S-EGCG complexes. The 11S-EGCG and 7S-EGCG complexes had more compact microstructure with a smooth surface than 11S and 7S proteins, while the microstructure of the complexes became undesirable with the increase of NaCl concentration. These results will lay the foundation for the development 11S-EGCG and 7 S-EGCG complexes as a new food material in the food industry.

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