Regulation of catalytic properties of enzymes in inverse micellae

A triple system (inverse micellae) that simulates the membrane environment of the enzyme was studied. Inverse micellae were obtained using anionic (ae rosol OT), synthetic (Brij 56), and natural (lecithin) surfactants. It was found that upon inclusion of an enzyme into inverse micellae, its activity can be regulated by changing the structure and nature of the surfactant mat rix. It was shown that enzyme activity in micellar environment is much high er than in water solution. Moreover, the enzyme solubilized in inverse mice llae (acid phosphatase) shows a superactivity, It was found that surfactant s specifically interact with solubilized enzyme, and the activity of the en zyme is inversely proportional to surfactant concentration The:mechanisms; of, viscotropic regulation of enzyme activity are discussed.