Development of new surfactants for protein extraction using reversed micelles

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Solvent extraction using reversed micelles provides an attractive to conventional procedures for the separation and purification of proteins from fermentation media and from very dilute solution. In the separation process, it is well known that a surfactant plays an important role, because solubilized proteins are stabilized by a surfactant layr. However, little attention has been paid to the design and synthesis of optimal surfactants for the protein extraction. In this study, new surfactants have been synthesized for potential use in reversed micellar protein extraction operations, and the following results were obtained :1.Preferential solubility of the surfactant in an aliphatic solvent such as hexane, heptane or iso-octane, and the formation of reversed micelles with solubilization of significant quantities of water can be achieved by using strongly hydrophobic, twin alkyl chains as the hydrophobic moiety.2.Different surfactants having identical water solubilizing capacities can have significantly different behavior in protein extractions, where extraction efficiency appears to be governed by the nature of the interfacial complex that forms between surfactants and proteins.3.Bulky surfactant chains provide a steric hindrance to the adsorption of the surfactant to the protein surface, thus inhibiting solvation of the protein/surfactant complex, and hence protein extraction. Under these conditions, a precipitate forms either in the bulk aqueous phase or at the interface. Surfactants that can from a close packed complex with the protein are excellent protein solubilizing agents. Dioleyl phosphoric acid (DOLPA) appears to be one of the best surfactants currently available for protein extraction.Now, we are studying more detail about extraction mechanism of proteins and novel application of newly developed reversed micelar sysytem.