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Proteins at interfaces are important for protein formulations and in soft materials such as foam. Here, interfacial stability and physicochemical properties are key elements, which drive macroscopic foam properties through structure-property relations. Native and fluorescein isothiocyanate-labeled bovine serum albumin (BSA) were used to modify air-water interfaces as a function of pH. Characterizations were performed with tensiometry and sum-frequency generation (SFG). SFG spectra of O-H stretching vibrations reveal a phase reversal and a pronounced minimum in O-H intensity at pH values of 5.3 and 4.7 for native and labeled BSA, respectively. This minimum is attributed to the interfacial isoelectric point (IEP) and is accompanied by a minimum in surface tension and negligible ζ-potentials in the bulk. Interfacial proteins at pH values close to the IEP can promote macroscopic foam stability and are predominately located in the lamellae between individual gas bubbles as evidenced by confocal fluorescence microscopy. Different from the classical stabilization mechanisms, for example, via the electrostatic disjoining pressure, we propose that the presence of more close-packed BSA, because of negligible net charges, inside the foam lamellae is more effective in reducing foam drainage as compared to a situation with strong repulsive electrostatic interactions.

Charge-Controlled Surface Properties of Native and Fluorophore-Labeled Bovine Serum Albumin at the Air–Water Interface