Characterization of β-lactoglobulin adsorption on silica membrane pore surfaces and its impact on membrane emulsification processes.

[Display omitted] Protein adsorption plays a key role in membrane fouling in liquid processing, but the specific underlying molecular mechanisms of β-lactoglobulin adsorption on ceramic silica surfaces in premix membrane emulsification have not been investigated yet. In this study, we aimed to elucidate the β-lactoglobulin adsorption and its effect on the premix membrane emulsification of β-lactoglobulin-stabilized oil-in-water emulsions. In particular, the conformation, molecular interactions, layer thickness, surface energy of the adsorbed β-lactoglobulin and resulting droplet size distribution are investigated in relation to the solvent properties (aggregation state of β-lactoglobulin) and the treatment of the silica surface (hydrophilization). The β-lactoglobulin adsorption is driven by attractive electrostatic interactions between positively charged amino acid residues, i.e. , lysin and negatively charged silanol groups, and is stabilized by hydrophobic interactions. The strong negative charges of the treated silica surfaces result in a high apparent layer thickness of β-lactoglobulin. Although the conformation of the adsorbed β-lactoglobulin layer varies with membrane treatment and the solvent properties, the β-lactoglobulin adsorption offsets the effect of hydrophilization of the membrane so that the surface energies after β-lactoglobulin adsorption are comparable. The resulting droplet size distribution of oil-in-water emulsions produced by premix membrane emulsification are similar for treated and untreated silica surfaces. [ABSTRACT FROM AUTHOR]