The possibility of modulating the mesoscopic properties of food colloidal systems by the dielectric constant is studied by determining the impact of small amounts of ethanol (10%) on the adsorption of egg white ovalbumin onto the air-water interface in the absence and presence of pectin. The adsorption kinetics was monitored using tensiometry. The addition of ethanol resulted in considerably slower adsorption of the protein onto the interface, and this effect was enhanced when the protein was in complex with the pectin. Time-resolved fluorescence measurements demonstrated that in the case of noncomplexed ovalbumin the addition of ethanol resulted in a more condensed protein surface layer where ovalbumin adopted a preferred orientation at the interface. In contrast, the effect of ethanol on the ovalbumin-pectin complex suggested a pronounced multipoint electrostatic interaction between protein and polyelectrolyte and the formation of a more rigid spatial arrangement within the complex, thereby leading to suppressed protein-protein interactions. From this work it is concluded that by the enhanced binding affinity between ovalbumin and pectin a strong effect on the adsorption properties of the protein can be accomplished. This work does therefore illustrate how solvent quality can be exploited effectively to enhance or suppress protein functional behavior in complex applications containing air-water interfaces.