Abstract
ABSTRACTPhase transfer experiments were performed, involving contact between an aqueous 1:1 solution of α‐lactalbumin and β‐lactoglobulin and an AOT‐in‐isooctane reversed micellar phase. The resulting extraction and separation of the two proteins were analyzed as functions of pH, ionic strength and total protein concentration using SDS‐PAGE, and compared with extractions from pure solutions. At low protein concentrations, the extent of reversed micellar solubilization of the two pure proteins predicted well the extraction from mixtures. However, at higher protein concentrations β‐lactoglobulin appeared to be excluded from the micellar droplets. Because of the significantly different partitioning behavior of the two proteins, reversed micellar extraction from an initially equal weight mixture led to an effective separation of the proteins.
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