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The Expression and Functional Analysis of Recombinant Alcohol Dehydrogenase
Analytical Science and Technology / Analytical Science and Technology, (P)1225-0163; (E)2288-8985
1999, v.12 no.6, pp.565-570
Kong,
K., Shim,
E., Park,
H., Kim,
E., Cho,
S., Park,
S., &
Kim,
Y.
(1999). The Expression and Functional Analysis of Recombinant Alcohol Dehydrogenase. Analytical Science and Technology, 12(6), 565-570.
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Abstract
The alcohol dehydrogenase (ADH) gene from Bacillus stearothermopilus was amplified by the polymerase chain reaction. The amplified DNA was inserted into the expression vector pGEX-KG, and expressed it as a fusion protein with glutathione S-transferase (GST) in E. coli. The recombinant ADH was produced by induction with 1 mM isopropyl-<TEX>${\beta}$</TEX>-D-thiogalactopyranoside at <TEX>$37^{\circ}C$</TEX> and purified by glutathione affinity chromatography. The recombinant ADH exhibited high substrate specificity for ethanol. The activity of the recombinant ADH proceeded optimally at pH 9.0 and <TEX>$70^{\circ}C$</TEX>. The recombinant ADH was highly stable against high temperature. This thermostable alcohol dehydrogenase can be used for the enzymatic determination of alcohol and for the industrial production of alcohol.
- keywords
- alcohol dehydrogenase, Bacillus stearothermopilus, expression in E. coli
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