Modulation of molecular state and air-water interface adsorption behavior of ovalbumin via interference with its surrounding charge distribution

Herein, pH combined with ionic strength was employed to modulate the charge distribution around ovalbumin molecules, and the whole process (from the water phase to the interface) of film formation and stabilization of ovalbumin at the air-water interface was further analyzed. As the pH continuously rose above the isoelectric point, the molecular surface charge increased. More cations, however, reduced the surface charge through the electrostatic shielding effect. The pH and cationic strength were shown to have a remarkable effect on the aggregate size. Intrinsic fluorescence and excitation emission matrix spectroscopy indicated that the migration of tryptophan and tyrosine was accompanied by a change in the backbone structure and rearrangement of the hydrophilic/hydrophobic side chains. Interfacial adsorption kinetic analysis revealed that low pH and ionic strength generally favored the adsorption and stabilization of ovalbumin. Lissajous plots confirmed that stronger intra-interfacial interactions and viscoelastic-like solid interfaces would be generated under the above conditions. Interfacial dilatational rheology analysis illustrated that in most cases, the interfacial film formed by ovalbumin was dominated by an elastic response and produced a nonlinear viscoelastic response under strain. Overall, the combined effect of low pH (pH 5.0) and ionic strength (25 mmol/L and 50 mmol/L) on the surface charge resulted in superior foam capacity (60.00% for pH 5.0 and 50 mmol/L) and stability (97.87% for pH 5.0 and 25 mmol/L). This study detailed the mechanism by which charge influenced the molecular and interfacial properties of ovalbumin, leading the way for the development of protein-based foam systems.