Entrapping of tyrosinase in a system of reverse micelles
The enzymatic activity of tyrosinase was studied both in aqueous and organic media. In the latter case tyrosinase was entrapped in a system of reverse micelles of Aerosol OT in octane. At hydration degree 25, when the inner cavity of the reverse micelles was comparable with the size of a tetrameric tyrosinase form known for aqueous solutions, an optimum level of catalytic activity was observed. An