REVERSE MICELLE SIZE DISTRIBUTION AND MECHANISM OF PROTEIN SOLUBILIZATION INTO REVERSE MICELLES

The mean size and distribution of reverse micelles prepared by dissolving Aerosol OT (AOT) in isooctane were measured by using a dynamic light-scattering method. The results were independent of AOT concentration and were correlated with water content, which was controlled by salt concentration in the bulk aqueous phase. A simple scheme for solubilization of proteins into micelle solution is presented. It assumes that the proteins adsorbed on the interface between aqueous and organic solutions may dissolve into the micelles when they encounter micelles of greater size than those of the proteins. The effect of the steric and electrostatic interaction between the micelles and proteins is also taken into account. Separation of lysozyme, α-chymotrypsin and BSA was carried out as an application of the present solubilization scheme. © 1990, The Society of Chemical Engineers, Japan. All rights reserved.