Interfacial curcumin complexation by facile oil-dispersion remodels protein profile and mechanics to tailor emulsion stability of poultry liver proteins

This study revealed that the interfacial and emulsifying behaviors of native chicken (CLP-n), duck (DLP-n), and goose (GLP-n) liver proteins could be improved by facilely oil dispersion using curcumin (CLP-Cur, DLP-Cur, GLP-Cur). The inherent structural flexibility of CLP-n enabled superior initial interfacial adsorption, a trait further amplified by interfacial curcumin complexation via hydrophobic interactions. While curcumin generally strengthened all interfaces, its effect was most synergistic with CLP, rendering CLP-Cur the most elastic (16.20 mN/m) and robust interfacial film. Crucially, proteomic analysis revealed that curcumin selectively reshaped the interfacial protein profile, enriching high-affinity proteins ( e.g. , hemoglobin and Annexin A5) in CLP-Cur while rigid proteins ( e.g. , actin) dominated DLP-Cur and GLP-Cur. This molecular reprogramming directly transitioned CLP-Cur emulsions the finest droplets and highest storage stability. This work establishes curcumin complexation as a facile strategy to improve emulsion stability and valorize poultry liver by-products by primarily reconstituting interfacial architecture. • Chicken liver protein’s higher flexibility enhances interfacial adsorption and elasticity • Curcumin complexation remodels interfacial layer with high affinity proteins, e.g. , hemoglobin • Chicken liver protein-curcumin complex forms most robust and elastic interfacial film • It yields emulsion with finest droplets and highest stability than duck/goose protein complexes