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-ethylbenzthiazoline-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.