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β-Lactoglobulin as a nanotransporter for glabridin: xxploring the binding properties and bioactivity influences

Wei, Y., Vriesekoop, F., Yuan, Q. and Liang, H. (2018) β-Lactoglobulin as a nanotransporter for glabridin: xxploring the binding properties and bioactivity influences. ACS Omega, 3 (9). pp. 12246-12252.

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Official URL: https://doi.org/10.1021/acsomega.8b01576

Abstract

ABSTRACT: Based on the fact that β-lactoglobulin (β-lg) can solubilize readily in water and bind many small hydrophobic molecules, a novel nanocomplexed glabridin with β-lg was developed by an antisolvent precipitation method. After binding to β-lg, the solubility of glabridin in aqueous solution was enhanced 21 times. Fluorescence spectroscopy of β-lg revealed that the interaction of glabridin with β-lg made the environment of Trp and Tyr residues on β-lg more hydrophilic. The morphology and crystal form of the nanocomplexed glabridin with β-lg was characterized and the changes in β-lg conformation was also been investigated. In combination with molecular docking modeling, the results revealed that glabridin was bound to β-lg by hydrophobic forces and hydrogen-bond interactions. Furthermore, the nanocomplexed glabridin with β-lg had a better 2,2-diphenyl-1-picrylhydrazyl radical-scavenging capacity and 2,2′-azino-bis-3-ethylbenzthiazo- line-6-sulfonic acid radical-scavenging capacity compared to free glabridin at the same concentration during in vitro tests. Thus, nanocomplexing with β-lg, by virtue of its ability to enhance the solubility of glabridin in aqueous systems, provides a suitable opportunity as a nanocarrier molecule.

Item Type: Article
Divisions: Food Science and Agri-food Supply Chain Management
Depositing User: Ms Kath Osborn
Date Deposited: 02 Jan 2019 12:41
Last Modified: 02 Jan 2019 12:43
URI: http://hau.collections.crest.ac.uk/id/eprint/17367

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