Protein adsorption and interfacial rheology interfering in dilatational experiment

The static and dilatational response of β-lactoglobulin fibrils and native β-lactoglobulin (monomers) at water-air and water-oil interfaces (pH 2) was measured using the pendant drop method. The resulting adsorption behavior and viscoelasticity is dependent of concentration and adsorption time. The interfacial pressure of the β-lactoglobulin fibrils obtained in static measurements was 16–18 mN/m (against air) and 7 mN/m (against oil) for all concentrations. With higher concentrations, faster adsorption kinetics and slightly higher interfacial and surface pressure is achieved but did not lead to higher viscoelastic moduli. The transient saturation of the interface is similar for both the fibril solution and the monomers, however the fibril solution forms a strong viscoelastic network. To evaluate the superimposed adsorption behavior and rheological properties, the formed interfacial layer was subjected to dilatational experiments, which were performed by oscillating the surface area of the drop in sinusoidal and sawtooth (diagonal) deformation manner. The sinusoidal oscillations (time depended area deformation rate) result in a complex interfacial tension behavior against air and oil interfaces and show remarkable differences during compression and expansion as emphasized by Lissajous figures. For diagonal (constant area deformation rate) experiments, a slight bending of the interfacial tension response was observed at low frequencies emphasizing the influence of protein adsorption during rheological measurements.