A lipophilic protein nanoparticle (LPP) was fabricated by ultrasonication of the soy lipophilic protein (LP), which contains hydrophobic proteins and phospholipids. This LPP (Rh = 136 ± 0.8 nm, ζ-potential = -20 mV, pH 7.0) had an improved dispersibility and acted as an emulsifier. The oil/water (O/W) emulsion stabilized by this LPP exhibited superior physical stability over long-term storage (8 weeks), during a stress storage test (200 mM NaCl addition and heating at 90 °C), and in the presence of Tween 20 (1.0-4.0 wt %), in contrast to those emulsions stabilized by β-conglycinin and glycinin. Langmuir-Blodgett method and interface pressure determination revealed that LPP formed rigid and rough granular film at air/water interface. The excellent stability of emulsions stabilized by LPP highlights the synergic effect between hydrophobic proteins and phospholipids. These findings suggest that the complexes of hydrophobic protein aggregates and biosurfactant could form a stable interface which could be developed into a novel strategy to fabricate a stable food emulsion.