Kinetic Properties of Enzymes in AOT-Isooctane Reversed Micelles

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The rates of the α-chymotrypsin-catalyzed hydrolysis of N-glutaryl-L-phenylalanine p-nitroanilide(GPNA)and the 3α, 20β-hydroxysteroid dehydrogenase(HSDH)-catalyzed reduction of progesterone were measured and the dependence of the reaction rates on pH, concentrations of bis(2-ethylhexyl)sodium sulfosuccinate(AOT) and water, hydration ratio W_0(=[H_2O]/[AOT])and micellar diameter was studied. In both reaction systems, the maximum rates of the reactions catalyzed by the enzyme solubilized in reversed micelles exceeded those measured in bulk aqueous solutions. In particular, the rate of the HSDH-catalyzed reduction in the reversed micellar system was 750-fold greater than that in the bulk aqueous solution. THe optimum pH of the HSDH-catalyzed reduction in the reversed micellar system was almost unchanged from that in the bulk squeous solution, while the optimum pH of the α-chymotrypsin-catalyzed hydrolysis in the reversed micellar system shifted to higher pH values by 3 pH-units compared with that in the bulk aqueous solution. Even if the hydration ratio W_0 was kept constant, the rates of both reactions in the reversed micellar system were dependent on[AOT]and[H_2O]. However, the dependence of the rates of the HSDH-catalyzed reaction on[AOT]or[H_2O]was opposite to that of the α-chymotrypsin-catalyzed hydrolysis. Furthermore, the average micellar diameter depended on the individual values of[AOT]and[H_2O]and was not a kye controlling factor of the reaction rates.
公益社団法人日本生物工学会の論文
1990-12-25

Kinetic Properties of Enzymes in AOT-Isooctane Reversed Micelles

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