Adsorption of Hydrophobin-Protein Mixtures at the Air-Water Interface: The Impact of pH and Electrolyte

The adsorption of the proteins beta-casein,,6lactoglobulin, and hydrophobin, and the protein mixtures of beta-casein/hydrophobin and,beta-lactoglobulin/hydrophobin have been studied at the air-water interface by neutron reflectivity, NR. Changing the solution pH from 7 to 2.6 has relatively little impact on the adsorption of hydrophobin or lactoglobulin, but results in a substantial change in the structure of the adsorbed layer of beta-casein. In beta-lactoglobulin/hydrophobia mixtures, the adsorption is dominated by the hydrophobin adsorption, and is independent of the hydrophobin or beta-lactoglobulin concentration and solution pH. At pH 2.6, the adsorption of the beta-casein/hydrophobin mixtures is dominated by the hydrophobia adsorption over the range of beta-casein concentrations studied. At pH 4 and 7, the adsorption of,beta-casein/hydrophobin mixtures is dominated by the hydrophobin adsorption at low beta-casein concentrations. At higher beta-casein concentrations, beta-casein is adsorbed onto the surface monolayer of hydrophobin, and some interpenetration between the two proteins occurs. These results illustrate the importance of pH on the intermolecular interactions between the two proteins at the interface. This is further confirmed by the impact of PBS, phosphate buffered saline, buffer and CaCl2 on the coadsorption and surface structure. The results provide an important insight into the adsorption properties of protein mixtures and their application in foam and emulsion stabilization.