ArticleFrontiers in nutrition2022
Changes on the conformational and functional properties of soybean protein isolate induced by quercetin.
Article in Frontiers in nutrition, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed, 34 citations in OpenAlex.
- Polymerization degree-driven impact on digestive enzyme inhibition by proanthocyanidins: mechanistic insights.Food chemistry: X · 2026Article
- Thermogelling Hydrogel for Sustained Topical Delivery of Quercetin for the Treatment of Atopic Dermatitis.AAPS PharmSciTech · 2026Article
- Structure and Functional Properties of Proteins from Different Soybean Varieties as Affected by the 11S/7S Globulin Ratio.Foods (Basel, Switzerland) · 2025Article
- Non-covalent interaction of sacha inchi protein and quercetin: Mechanism and physicochemical property.Food chemistry: X · 2025Article
- Inhibitory Activity of Quercetin, Rutin, and Hyperoside against Xanthine Oxidase: Kinetics, Fluorescence, and Molecular Docking.Current pharmaceutical biotechnology · 2025Article
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Authors and funding
11 authors at 2 institutions in 1 country.
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Abstract
The conformational changes and functional properties of SPI induced by quercetin was investigated via fourier transform infrared (FTIR) spectroscopy, fluorescence spectroscopy, circular dichroism (CD) spectroscopy and molecular docking. A decrease in the fluorescence intensity and a blue shift in the maximum wavelength were observed due to the binding process with fluorescent residues. The analysis of Stern-Volmer equation showed that the fluorescence quenching induced by quercetin took the form of static quenching, and the binding stoichiometry between SPI and quercetin was 1:1. The values of ΔH and ΔS were both positive illustrating that hydrophobic interaction was the primary binding force between quercetin and SPI. Results of FTIR and CD indicated that the binding with quercetin changed the secondary structure of SPI, resulting in a partially unfolded and more flexible structure. SDS-PAGE confirmed there was no covalent interaction between the two constituents. Molecular docking demonstrated that there were stable configurations and high matching degrees in both 11S and 7S proteins with quercetin via hydrogen bonds and hydrophobic interactions. Meanwhile, modification by quercetin enhanced the foaming and emulsifying capacities of SPI. These findings might provide theory reference for elucidation the mechanism of polyphenols-proteins interaction and development of related food additive products in future.
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