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KMID : 0380019950100010030
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Korean Journal of Biotechnology and Bioengineering
1995 Volume.10 No. 1 p.30 ~ p.36
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Purification and Characterization of Alcohol Dehydrogenase from Acetobacter sp. KM
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Abstract
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Membrane-bound alcohol dehydrogenase (ADH) was purified to homogeneity from.the acetic acid producing bacteria, Acetobacter sp. KM. The enzyme was solubilized and extracted with Triton X-100 and purified using the Mono-Q ion exchange chromatography and Superose 12 gel filtration chromatography. The enzyme was purified to 12-fold with a yield of 30%. The molecular weight of the purified enzyme was to be 335 KDa. SDS-PAGE of the enzyme showed two subunits with molecular weights of 79 KDa and 49 KDa. It indicated that the enzyme consisted of three subunits of the 79 KDa and two subunits of the 49 KDa. The purified ADH preferentially oxidized straight chain aliphatic alcohols except methanol. Formaldehyde, acetaldehyde and, glutaraldehyde were also oxidized. The apparent Km f or ethanol was 1.04 mM and the optimum pH and temperature were 5.0^-6.0 and 32 C, respectively. V 205 and divalent cations such as ZnC12 and NiCl2 inhibited enzymatic activity.
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