High-performance emulsions via phosphorylated HDL/phosvitin interface engineering: Characterization, stability, and curcumin protection.

Egg yolk proteins have garnered significant attention from researchers due to their outstanding functional properties, and physical modification methods serve as a key approach to enhancing the characteristics of these proteins. In this study, phosphorylated egg yolk high-density lipoprotein (HDL) was prepared using sodium tripolyphosphate (STP) to investigate the properties of the high-internal-phase emulsion formed after cross-linking with phosvitin (Pv), as well as its protective effect on curcumin. Phosphorylation significantly enhanced the functional properties of HDL, with the 6% STP treatment yielding the highest phosphorus content (7.32 mg/g) in the resulting phosphorylated HDL (P-HDL). Structural analyses confirmed covalent phosphate binding, which reduced HDL particle size, induced protein unfolding, and exposed hydrophobic regions, thereby improving its emulsifying capacity and thermal stability. A composite stabilizer composed of phosphorylated HDL (P-HDL) and Pv was developed to construct high internal phase emulsions (HIPEs). These HIPEs also exhibited superior performance in curcumin delivery, increasing its bioaccessibility to 38.10% compared with 15.40% in the control, while effectively inhibiting lipid oxidation during storage. This study provides a promising strategy for designing high-performance emulsion delivery systems.