Correlation between Physico-Chemical Characteristics of Particulated β-Lactoglobulin and Its Behavior at Air/Water and Oil/Water Interfaces

It is widely accepted that protein-based particles can efficiently stabilize foams and emulsions. However, it is not fully elucidated which particle properties are decisive for the stabilization of air/water and oil/water interfaces. To unravel this correlation, selected properties of nano-sized soluble beta-lactoglobulin particles were changed one at a time. Therefore, particles of (1) variable size but similar zeta potential and degree of cross-linking and (2) similar size but different further properties were produced by heat treatment under a specific combination of pH value and NaCl concentration and then analyzed for their interfacial behavior as well as foaming and emulsifying properties. On the one hand, it was found that the initial phase of protein adsorption at both the air/water and the oil/water interface was mainly influenced by the zeta potential, independent of the particle size. On the other hand, foam stability as resolved from the time-dependent evolution of mean bubble area negatively correlated with disulfide cross-linking, whereas emulsion stability in terms of oil droplet flocculation showed a positive correlation with disulfide cross-linking. In addition, flocculation was more pronounced for larger particles. Concluding from this, foam and emulsion stability are not linked to the same particle properties and, thus, explanatory approaches cannot be used interchangeably.

Automated summary

Protein adsorption at both air/water and oil/water interfaces is mainly influenced by zeta potential, independent of particle size. Foam stability is negatively correlated with disulfide cross-linking, while emulsion stability shows a positive correlation with disulfide cross-linking, especially for larger particles. Foam and emulsion stability are not linked to the same particle properties, and explanatory approaches cannot be used interchangeably.