Changes and roles of secondary structures of whey protein for the formation of protein membrane at soy oil/water interface under high-pressure homogenization.

The conformational changes of whey proteins upon adsorption at the soy oil/water interface were investigated using Fourier transform infrared (FT-IR) spectroscopy. Significant changes were observed in the bands assigned to beta-sheets and alpha-helix structures following the adsorption of proteins at the oil/water interface. The remaining interfacial proteins after Tween 20 desorption revealed small changes in beta-sheet and alpha-helical structures, whereas in the desorbed whey proteins the unordered structures largely increased, and beta-sheet structures almost disappeared. These FT-IR results provide important knowledge about the conformational modifications in whey proteins occurring upon adsorption at the oil/water interface. Finally, specific conformational changes are necessary to stabilize emulsions: adsorption-induced unfolding, increase in alpha-helical structures to establish interactions with the oil phase, and aggregation between adsorbed whey proteins to form protein membranes. Moreover, the structural changes in whey protein adsorbed at the oil/water interface under high-pressure homogenization are irreversible.