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KMID : 0545119920020040268
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Journal of Microbiology and Biotechnology
1992 Volume.2 No. 4 p.268 ~ p.272
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Specificity of Alcohol Dehydrogenase from Clostridium acetobutylicum ATCC 4259
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Kim Byung-Hong
J. Gregory Zeikus
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Abstract
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Alcohol dehydrogenase activity of Clostridium acetobutylicum ATCC 4259 was studied for its specificity against substrates in acidogenic and solventogenic cultures. The bacterium reduces propionate, valerate and caproate added to the medium to the corresponding alcohols. Acetaldehyde, propionaldehyde, butyraldhyde, pentanal, and hexanal were used as the substrates by alcohol dehydrogenase, and all were reduced to the corresponding alcohols with varying affinities and reaction velocities. Acetaldehyde showed the lowest affinity and lowest velocity while the other aldehydes showed similar K_m and V_max values. NADPH was used as the electron donor for the reduction of aldehydes. Alcohol dehydrogenase activity was low in acidogenic culture, and high in solventogenic culture.
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KEYWORD
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