[Regulation of catalytic properties of enzymes in "inverse micelles"]. / Reguliatsiia kataliticheskikh svoistv fermenta v "obrashchennykh mitsellakh".

A triple system (inverse micellae) that simulates the membrane environment of the enzyme was studied. Inverse micellae were obtained using anionic (aerosol 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 matrix. It was shown that enzyme activity in micellar environment is much higher than in water solution. Moreover, the enzyme solubilized in inverse micellae (acid phosphatase) shows a superactivity. It was found that surfactants specifically interact with solubilized enzyme, and the activity of the enzyme is inversely proportional to surfactant concentration. The mechanisms of viscotropic regulation of enzyme activity are discussed.