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KMID : 0366119860140040337
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Korean Journal of Applied Microbiology & Bioengineering
1986 Volume.14 No. 4 p.337 ~ p.338
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韓國産業微生物學會
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Abstract
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The fundamental studies concerning the horse liver alcohol dehydrogenase(IILADII) in AO´r isooctane micellar system were carried out. When enzyme activity was determined by the rate of increase in fluorescence intensity of NADII, two different slopes were observed and this could be due to the substrate transfer limitation across the interface. As increasing the car-bon number of primary alcohol, enzyme activity and the ratio between two slopes decreased except for heptanol and octanol. In order to understand the enzyme reaction kinetics in reverse micelles, the mass transfer effects on the kinetic constant were studied by theoretical analysis. In the case of Michaelis-Menten kinetics, the apparent maximum reaction rate is not changed, but the apparent Michaelis constant increases with increasing substrate transfer limitation and is inversely proportional to the partition coefficient of substrate. Our approach could well explain the mass transfer effect on the kinetics of an enzyme action in reverse micelles and reveal the system characterized by low mass transfer rate.
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KEYWORD
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