Mechanism of enhancing the water-solubility and stability of curcumin by using self-assembled cod protein nanoparticles at an alkaline pH.

Curcumin (Cur) is a bioactive phytochemical which is claimed to have several health-promoting benefits, whose applications are challenging due to its poor water-solubility, chemical instability, and low bioavailability. In this research, Cur was encapsulated in the cod protein (CP) using a pH-driven method to enhance its solubility and stability. The physicochemical and structural properties of cod protein-curcumin nanoparticles (CP-Cur) formed were characterized. Fluorescence spectroscopy (FL), ultraviolet spectroscopy (UV), circular dichroism (CD), and dynamic light scattering (DLS) results collectively suggest that the protein originally with a molten-globule state refolded into a more ordered structure after neutralization, during which Cur was incorporated. Fluorescence quenching and isothermal titration calorimetry (ITC) further showed that the CP/Cur binding was mainly driven by hydrophobic interactions, resulting in static fluorescence quenching and energy release. Up to 99.50% of Cur was loaded in the CP delivery system. Furthermore, the thermal stability and photostability of Cur were greatly improved due to the protection of the protein. The present study proved that cod protein could be a great potential edible carrier for encapsulating curcumin.