1. Study of the mechanism of non-covalent interactions between chlorogenic acid and soy protein isolate: Multi-spectroscopic, in vitro, and computational docking analyses.
- Author
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Ma N, Duan J, Zhou G, and Wang X
- Subjects
- Hydrophobic and Hydrophilic Interactions, Hydrogen Bonding, Protein Structure, Secondary, Spectrometry, Fluorescence, Protein Binding, Antioxidants chemistry, Soybean Proteins chemistry, Soybean Proteins metabolism, Chlorogenic Acid chemistry, Molecular Docking Simulation
- Abstract
This study investigated the interaction mechanism between chlorogenic acid (CA) and soy protein isolate (SPI) through multi-spectroscopic and computational docking and analyzed the changes in its functional properties. The results showed that the interaction of CA with SPI changed its UV and fluorescence absorption, and the fluorescence quenching mechanism was static quenching. At the same time, the secondary structure of the protein was altered, with a reduction in α-helix, β-sheet and β-turn. Computer docking analysis showed that CA binds to SPI through hydrophobic interactions, van der Waals forces, and hydrogen bonding to form a more compact complex. In addition, the dose-dependent enhancement of CA improved the functional properties of the complexes, including foaming, emulsification, and antioxidant properties. This study systematically investigated the mechanism of interaction between CA and SPI, which supports further research on food complex systems containing CA and SPI, as well as the application of the complex., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2023. Published by Elsevier Ltd.)
- Published
- 2024
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