Reverse micelles and protein biotechnology

Abstract

Reverse micelles are nanometer-sized (1-10 nm) water droplets dispersed in organic media obtained by the action of surfactants. Surfactant molecules organize with the polar part to the inner side able to solubilize water and the apolar part in contact with the organic solvent. Proteins can be solubilized in the water pool of reverse micelles. Studies on the structure-function relationships of proteins in reverse micelles are very important since the microenvironment in which the protein is solubilized has physico-chemical properties distinct from a bulk aqueous solution. Some of the unique characteristics of reverse micelles make them very useful for biotechnological applications. Charge and hydrophilic/hydrophobic characteristics of the protein and the selection of surfactant can be used to achieve selective solubilization of proteins. This has been used to extend the classical liquid-liquid extraction with solvents to protein bioseparation. For biocatalysis the presence of a bulk organic solvent allow synthetic reactions to be performed via the control of water content and the solubilization of hydrophobic substrates. This is accomplished with a higher interfacial area (about 100 m2/mL) than the conventional biphasic systems, minimizing mass transfer problems.