Pickering emulsions stabilized by reassembled oleosome protein nanoparticles for co-encapsulating hydrophobic nutrients

In this study, oleosome proteins were disassembled using guanidine hydrochloride to form shell-core colloidal particles (reassembled oleosome proteins, ROPs). These particles were then used to prepare a dual-compartment-structured Pickering emulsion to co-deliver curcumin (Cur) and vitamin D. The results showed that ROP can effectively encapsulate Cur inside the hollow structure. Moreover, at a Cur concentration of 100 mu M, the ROP-Cur contact angle was 71.5 degrees, which aids the preparation of stable Pickering emulsions. The most stable Pickering emulsion was then prepared by adjusting the ROP-Cur emulsifier and oil phase concentrations. The Pickering emulsion prepared with 2.0 mg/mL emulsifier and the addition of 10% oil phase displayed the best stability, with an average particle size, zeta-potential, and Turbiscan Stability Index of 2.2 mu m,-31.5 mV, and 3.63, respectively. Notably, the emulsification process doesn't destroy the shell-like structure of ROP-Cur. Instead, it triggers the aggregation of ROP-Cur, which is finally adsorbed at the oil-water interface. Our designed strategy successfully affords double-compartment microdroplets and improves the storage stability of biologically active compounds.

Automated summary

In this study, oleosome proteins were disassembled to form shell-core colloidal particles, which were then used to prepare a dual-compartment-structured Pickering emulsion for co-delivery of curcumin and vitamin D. The resulting Pickering emulsion exhibited excellent stability and maintained the shell-like structure of oleosome proteins. The designed strategy successfully achieved double-compartment microdroplets and improved the storage stability of biologically active compounds.