THE PRINCIPLES OF ENZYME STABILIZATION .6. CATALYSIS BY WATER-SOLUBLE ENZYMES ENTRAPPED INTO REVERSED MICELLES OF SURFACTANTS IN ORGANIC-SOLVENTSстатья
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Дата последнего поиска статьи во внешних источниках: 29 мая 2015 г.
Аннотация:1.1. The possibility of stabilizing water-soluble enzymes againsts the inactivating action of organic solvents by means of surfactants has been studied. Several enzymes (О±-chymotrypsin (EC 3.4.21.1), trypsin (EC 3.4.21.4), pyrophosphatase (EC 3.6.1.1), peroxidase (EC 1.11.1.7), lactate dehydrogenase (EC 1.1.1.27) and pyruvate kinase (EC 2.7.1.40)) were used to demonstrate that enzymes can be entrapped into reversed micelles formed by surfactants (Aerosol OT, cetyltrimethylammonium bromide, Brij 56) in an organic solvent (benzene, chloroform, octane, cyclohexane). The enzymes solubilized in this way retain their catalytic activity and substrate specificity. 2. 2.|A kinetic theory has been put forward that describes enzymatic reactions occurring in a micelle-solvent pseudobiphasic system. In terms of this theory, an explanation is given for the experimental dependence of the Michaelis-Menten equation parameters on the concentrations of the components of a medium (water, organic solvent, surfactant) and also on the combination of the signs of the charges in the substrate molecules and on interphase (++, +-, –). 3. 3.|The results obtained by us may prove important for applications of enzymes in organic synthesis and for studying the state and role of water in the structure of biomembranes and active centres of enzymes