Role of the Interface in Protein Extractions Using Nonionic Microemulsions

Abstract

The oil–water interface is thought to have a significant role in the extraction of proteins into nonionic microemulsions. Several surfactants, that have a known specificity for particular proteins, have been tested for their ability to improve the specificity of Neodol 91-2.5 (linear alcohol ethoxylate) microemulsions. Only some of these protein-specific surfactants were capable of improving specificity. In successful extractions, a minimum amount of protein-specific surfactant has to be added to Neodol 91-2.5 nonionic microemulsion before any protein is extracted. Above this minimum, all of the protein is removed. It was also observed that below this minimum the protein-specific surfactant is present at the oil–water interface, but is not available for protein extraction. This is in contrast with affinity-based reverse micellar extraction where the appearance of the ligand at the oil–water interface is sufficient to cause protein extraction. The physical structure of the interface plays a role in the protein–surfactant interactions seen in nonionic microemulsions. Two criteria need to be satisfied as a basis for successful protein extraction. A minimum headgroup area of the protein-specific surfactant, and a minimum fractional area coverage of the protein-specific surfactant at the oil–water interface, are simultaneously required for protein extraction. A conceptual model has been proposed to explain these observations.