Journal
FOOD BIOSCIENCE
Volume 47, Issue -, Pages -Publisher
ELSEVIER
DOI: 10.1016/j.fbio.2022.101673
Keywords
Mucin; alpha-amylase; Spectroscopy; Molecular docking; Virgin olive oil polyphenols
Categories
Funding
- National Natural Science Foundation of China [31901728]
- Jiangsu Planned Projects for Postdoctoral Research Funds [2020Z297]
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This study investigated the interaction mechanism of mucin and alpha-amylase with polyphenols in virgin olive oil through various spectroscopic methods and molecular docking, revealing a static quenching mechanism and conformational changes in mucin. Molecular docking also predicted the binding sites of polyphenols with human salivary mucin and alpha-amylase.
The interaction mechanism of mucin and alpha-amylase with virgin olive oil (VOO) polyphenols (oleuropein (OL), tyrosol (TY), hydroxytyrosol (HT)) was analyzed by fluorescence, ultraviolet (UV) absorption, attenuated total reflection Fourier transform infrared (ATR-FTIR), circular dichroic (CD) spectroscopy and molecular docking. A total of 17 polyphenols have been identified in the selected VOO, and the TY, HT and OL were the main compounds. The quenching mechanism between mucin/alpha-amylase and three VOO polyphenols was static, mainly through van der Waals forces and hydrogen bonds. The results of UV absorption, ATR-FTIR, and CD spectroscopy revealed that the conformation of mucin changed after combining with the three polyphenols, while that of the alpha-amylase changed little. Molecular docking predicted the interaction sites of the three polyphenols with human salivary mucin and alpha-amylase. The present study could provide the theoretical foundation for further research on the interaction between human salivary protein and phenolic compounds in VOO.
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