Enhanced interfacial stabilization of high internal phase emulsion using goose liver protein via ultrasonication...

The interfacial complexation between goose liver protein (GLP) and oily dispersed curcumin in impacting the protein interfacial dynamics and high internal phase emulsions (HIPEs) stabilization was validated. Results from surface hydrophobicity, size, atomic force microscopy, and fluorescence quenching showed that pre-ultrasonication (100 W, 300 W and 500 W) conduced to pronounced heterogeneous hydrophobic interaction that elevated GLP adsorption and association at the interface. The synergistic curcumin complexation with medium ultrasonication (300 W_+Cur) maximized GLP interfacial deposition and elasticity (11.58 and 32.80 mN/m for π₁₀₈₀₀ and E_d) due to most sufficient GLP unfolding. The HIPE for 300 W_+Cur gave the highest network intersection with densely packed droplets from the lowest D [4,3] (38.17 ± 0.20 μm) while highest oil holding (91.91 %) and rheological stability. Turbiscan stability index, TBARS and fatty acid profile suggested that the 300 W_+Cur displayed also the highest physiochemical stability (40 °C, 7 days) via sufficient oil enclosure and networking, as was also the case when oil polarity varied. This study reported firstly that the HIPEs stabilization could be tuned by interfacial GLP-curcumin complexation affinity (i.e., through protein pre-ultrasonication), which could potentiate GLP based HIPEs with tailored rheological and mechanical properties for applications.