ACTIVATION AND STABILIZATION OF ENZYMES ENTRAPPED INTO REVERSED MICELLES - STUDIES ON HYDROLYZING ENZYMES - PROTEASE AND ALPHA-AMYLASE

Observations of the activity of two hydrolyzing enzymes-protease and a lpha-amylase-entrapped inside the reversed micelles formed by surfacta nts in hexane, benzene, and cyclohexane are reported. The surfactants chosen for this study are: Tween 80, a nonionic surfactant, Cetyl pyri dinium chloride, a cationic surfactant, and two anionic surfactants, s odium lauryl sulfate and Aerosol OT. Tween 80 enhances the activity of both protease and alpha-amylase. Sodium lauryl sulfate and Aerosol OT , which are ionic surfactants, enhance the activity of protease, but i nhibit the activity of alpha-amylase. Cetyl pyridinium chloride, howev er, enhances the activity of alpha-amylase, but inhibits the activity of protease. Enhanced activity is generally severalfold greater in com parison to the activity observed in the usual aqueous system in the ab sence of reversed micelles. It has also been observed that the enhance d activity of the enzymes entrapped inside the reversed micelles remai ns preserved for a much longer period of time in comparison to the act ivity 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 ov ertones.