Since it appears possible to use active biomolecules outside a natural environment, and even more so since genetic engineering enables the production by recombinant microorganisms or animal cell cultures of more and more various proteins, a great deal of investigation has been carried out in order to separate and purify these compounds from complex medium broths. Due to the continually renewed diversity and complexity of proteins and media, a simple scheme of extraction and purification process does not exist, each example being a specific case for which, usually, a sequence of several techniques must be developed, depending on the properties of the protein, the nature of the impurities and the final purity demanded.Extraction of proteins using reversed micelles emerges as a new and attractive technique (1-4) in terms of selectivity and concentration. It presents a close similarity with liquid-liquid extraction since both are diphasic processes which consist of partitioning a targeted solute between an aqueous feed phase and an organic phase and then operate the back transfer to a second aqueous stripping phase. The yield and selectivity of the separation is determined by thermodynamic properties at equilibrium. However, classical organic solvents are not suitable to achieve the extraction of most proteins which are hydrophilic molecules and, therefore, insoluble in apolar solvents. Moreover, due to their low polarity, organic solvents modify the interactions which stabilize the native protein conformation, leading to its denaturation. In order to extract and preserve the protein, it is necessary to maintain its aqueous environment by adding a surfactant which aggregates in apolar solvent and