The interfacial transport processes of proteins from a reverse micellar phase to an aqueous phase have been investigated focusing on micellar-micellar interaction. The proteins solubilized into reverse micelles were backextracted to the aqueous phase depending on the concentration of reverse micelles in organic phase. This fact seems to suggest the importance of micellar-micellar interactions in back-extraction processes. The interactions induced by various alcohol addition and temperature change could be evaluated easily and quantitatively by the percolation phenomena in reverse micellar systems (RVMS). The interactions were influenced considerably by the presence of small amount of alcohol and temperature in the RVMS. The addition of alcohols promotes the back-extraction of proteins depending on their species and concentrations. In particular, the alcohols that suppress the cluster formation of reverse micelles, remarkably improve the back-extraction processes. With a small amount of alcohol (20mM OctOH), Bovine carbonic anhydrase (CAB) can be back-extracted completely from reverse micelles to aqueous solution at the optimal temperature, in which the so high concentration of salt is not necessary.