Abstract
Loading hydrophobic bioactive with protein-based nanocarrier is challenged by inefficient encapsulation or colloidal instability. In this study, unfolding 11S globulin was induced by reducing disulfide bonds to form nanoparticles which served as effective nanocarriers for curcumin. Results revealed that 11S globulin unfolded after reducing treatment, as proved by the red-shifting in maximum fluorescence wavelength and the transitions of secondary structure. Disulfide-linked subunits progressively dissociated into their separate polypeptides and even vanished at high reductant concentrations. Reductant-treated 11S globulin was characterized by exposed hydrophobic regions, evidenced by the increased surface hydrophobicity and fluorescence quenching, which triggered the hydrophobic interaction between protein and curcumin. Finally, up to 98.77% of curcumin (0.5 mg/mL) could be encapsulated into 11S globulin nanoparticles. 11S-Cur complex exhibited superior thermal stability, with enhanced water solubility compared to the free curcumin. Accordingly, reducing treatment can be considered a facile and high-encapsulation-performance method to fabricate protein-based nanoparticles for embedding hydrophobic bioactive.
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