Micellar Enzymology: Superactivity of Enzymes in Reversed Micelles of Surfactants Solvated by Water/Organic Cosolvent Mixtures

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Abstract
Catalytic properties of α-chymotrypsin, peroxidase and laccase, dissolved in water-immiscible organic solvents by entrapping them into the reversed micelles of surfactants solvated by water/organic cosolvent (glycerol or 1,4- or 2,3-butanediol or dimethyl sulfoxide) mixtures, are studied. As micelle-forming surfactants, sodium salt of bis(2-ethylhexyl)sulfosuccinate (Aerosol OT) in n-octane or cetyltrimethylammonium bromide in n-octane/chloroform (1 : 1 by volume) mixture are used. The dependences of the catalytic activity on the surfactant solvation degree are bell-shaped. Maxima of the catalytic activity of enzymes solubilized in the micellar systems are observed at such optimum values of the surfactant solvation degree at which the size of micellar inner cavity and of the entrapped protein molecule is approximately equal. With decreasing content of water in the micellar media studied, the catalytic activity of the solubilized enzymes increases considerably, and is much (10-100 times) higher than in bulk aqueous buffers. In conclusion, possible mechanisms of the micellar effects are suggested.

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