ACTIVATION AND STABILIZATION OF INVERTASE ENTRAPPED INTO REVERSED MICELLES OF SODIUM LAURYL SULFATE AND SODIUM TAUROGLYCOCHOLATE IN ORGANIC-SOLVENTS

We report our observations on the activity of invertase enzyme entrapped inside the reversed micelles formed by either sodium tauroglycocholate or sodium lauryl sulfate in various organic solvents, namely hexane, n-decanol, benzene and carbon tetra-chloride. In this case more than four-fold increase in activity was observed under mild conditions in comparison to the activity in usual aqueous medium. Reversed micelles entrapped invertase exhibited higher velocity, low K//M value and longer active life as compared to enzyme in aqueous phase. This is in support of the view that surfactant stabilizes active conformation of enzyme by entrapping them. The interior of the reversed micelle acts like a microreactor that provides favorable aqueous microenvironment for the enzyme activity.