The complexity and high sensitivity of proteins to environmental factors give rise to a multitude of variables, which affect the stabilization mechanisms in protein foams. Interfacial and foaming properties of proteins have been widely studied, but the reported unique effect of pH, which can be of great interest to applications, has been investigated to a lesser extent. In this paper, we focus on the impact of pH on the stability of black foam films and corresponding foams obtained from solutions of a model globular protein—the whey β-lactoglobulin (BLG). Foam stability was analyzed utilizing three characteristic parameters (deviation time, transition time and half-lifetime) for monitoring the foam decay, while foam film stability was measured in terms of the critical disjoining pressure of film rupture. We attempt to explain correlations between the macroscopic properties of a foam system and those of its major building blocks (foam films and interfaces), and thus, to identify structure-property relationships in foam. Good correlations were found between the stabilities of black foam films and foams, while relations to the properties of adsorption layers appeared to be intricate. That is because pH-dependent interfacial properties of proteins usually exhibit an extremum around the isoelectric point (pI), but the stability of BLG foam films increases with increasing pH (3–7), which is well reflected in the foam stability. We discuss the possible reasons behind these intriguingly different behaviors on the basis of pH-induced changes in the molecular properties of BLG, which seem to be determining the mechanism of film rupture at the critical disjoining pressure.
Specific effects of Ca2+ions and molecular structure of β-lactoglobulin interfacial layers that drive macroscopic foam stability