Protein Extraction Using Reverse Micelles

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Abstract
The controlled solubilization of proteins in a reverse micelle-containing organic phase is considered as a method for separation of proteins by liquid-liquid extraction. Cytochrome-C was transferred between a bulk aqueous phase and a micellar phase, using the Aerosol OT-isooctane system of surfactant and solvent. It was observed that the extent of protein solubilization could be controlled by varying the ionic strength of the aqueous phase equilibrated with the micellar phase. The protein transferred into the micellar phase rapidly, under conditions of low ionic strength, and transferred out of the micelles relatively slowly, under conditions of high ionic strength. It is proposed that the effect of the ionic strength was to alter the electrostatic interaction between the surface charge of the protein and the charged interior of the reverse micelle by Debye screening.

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