Dual improvement in curcumin encapsulation efficiency and lyophilized complex dispersibility through ultrasound regulation of curcumin–protein assembly

Ultrasound has a recognized ability to modulate the structure and function of proteins. Discovering the influential mechanism of ultrasound on the intramolecular interactions of egg-white protein isolate–curcumin (EPI–Cur) nanoparticles and their intermolecular interaction during freeze drying and redispersion is meaningful. In this study, under the extension of pre-sonication time, the protein solubility, surface hydrophobicity, and curcumin encapsulation rate showed an increasing trend, reaching the highest value at 12 min of treatment. However, the values decreased under the followed extension of ultrasound time. After freeze drying and redispersion were applied, the EPI–Cur sample under 12 min of ultrasound treatment exhibited minimal aggregation degree and loss of curcumin. The retention and loading rates of curcumin in the lyophilized powder reached 96 % and 33.60 mg/g EPI, respectively. However, under excessive ultrasound of >12 min, scanning electron microscopy showed distinct blocky aggregates. Overexposure of the hydrophobic region of the protein triggered protein-mediated hydrophobic aggregation after freeze drying. X-ray diffraction patterns showed the highest crystallinity, indicating that the free curcumin-mediated hydrophobic aggregation during freeze drying was enhanced by the concentration effect and intensified the formation of larger aggregates. This work has practical significance for developing the delivery of hydrophobic active substances. It provides theoretical value for the dynamic dispersity change in protein-hydrophobic active substances during freeze drying and redissolving.