Activation and stabilization of enzymes entrapped into reversed micelles

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Abstract
Observations of the activity of two hydrolyzing enzymes—protease and α-amylase—entrapped inside the reversed micelles formed by surfactants in hexane, benzene, and cyclohexane are reported. The surfactants chosen for this study are: Tween 80, a nonionic surfactant, Cetyl pyridinium chloride, a cationic surfactant, and two anionic surfactants, sodium lauryl sulfate and Aerosol OT. Tween 80 enhances the activity of both protease and α-amylase. Sodium lauryl sulfate and Aerosol OT, which are ionic surfactants, enhance the activity of protease, but inhibit the activity of α-amylase. Cetyl pyridinium chloride, however, enhances the activity of α-amylase, but inhibits the activity of protease. Enhanced activity is generally severalfold greater in comparison to the activity observed in the usual aqueous system in the absence of reversed micelles. It has also been observed that the enhanced activity of the enzymes entrapped inside the reversed micelles remains preserved for a much longer period of time in comparison to the activity in the usual aqueous systems. These observations, which support the view that with proper choice of surfactant and the organic solvent, reversed micelles act like a microreactor that provides a favorable aqueous microenvironment for enzyme activity, have biotechnological overtones.