ABSTRACT
In this study, food-grade protein nanoparticles (Wild-NPs, α-lack-NPs, α'-lack-NPs, and (α + α')-lack-NPs) were organized as emulsion stabilizers via thermal induction. The effects of α and α' subunits in soybean protein isolate (SPI) on Wild nanoparticle Pickering emulsion (Wild-NPPEs), α-lack nanoparticle Pickering emulsion (α-lack-NPPEs), α'-lack nanoparticle Pickering emulsion (α'-lack-NPPEs) and (α + α')-lack nanoparticle Pickering emulsion ((α + α')-lack-NPPEs) were investigated. The Pickering emulsion stabilization mechanism indicated that the α'-lack-NPs particle size, surface hydrophobicity, and contact angle were mostly comparatively large. Therefore, the absence of the α' subunit made the desorption of protein nanoparticles at the oil and water interface require higher energy. Through the hydrophobic interaction between molecules, the structure and properties of the emulsion were improved, showing good stability. The existence of α'-lack-NPPEs leads to the formation of a gel-like network in the emulsion, which increases the viscosity of the emulsion and makes the network structure of the emulsion more uniform and denser.
