Experimental results evidenced that the non-ionic emulsifier replaces the protein on the interface (only a partial replacement was observed in the tested conditions) whereas the anionic molecule interacts with the protein forming complexes which can be almost completely replaced by the single emulsifier.
The interfacial layers are characterised by a prevalent solid-like behaviour, which proved to be similar to 3D weakly structured systems. The rheological properties are strongly dependent on the nature of both the emulsifier and the interface, nevertheless it was observed that ovalbumin yields a more structured and stronger layer than Admul and Tween. In mixed systems, increasing the emulsifier concentration, the extension of this 2D network decreases whereas the strength seems to be less dependent and evidences only a slight reduction for Admul addition at the A/W interface.