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The alcohol dehydrogenases (ADHs) from Lactobacillus kefir and Rhodococcus sp., which earlier turned out to be suitable for a chemoenzymatic one-pot synthesis with organocatalysts, were immobilized with their cofactors on a commercially available superabsorber based on a literature known protocol. The use of the immobilized ADH from L. kefir in the reduction of acetophenone as a model substrate led to high conversion (>95

作者:Giuseppe, Rulli;Marcel, Heidlindemann;Albrecht, Berkessel;Werner, Hummel;Harald, Gr?ger

来源:Journal of biotechnology 2013 年 168卷 3期

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作者:
Giuseppe, Rulli;Marcel, Heidlindemann;Albrecht, Berkessel;Werner, Hummel;Harald, Gr?ger
来源:
Journal of biotechnology 2013 年 168卷 3期
标签:
ADH Alcohol Alcohol dehydrogenase Enzyme catalysis Immobilization NAD(+) NADH NADP(+) NADPH Reduction alcohol dehydrogenase nicotinamide adenine dinucleotide oxidized form nicotinamide adenine dinucleotide phosphate oxidized form nicotinamide adenine dinucleotide phosphate reduced form nicotinamide adenine dinucleotide reduced form
The alcohol dehydrogenases (ADHs) from Lactobacillus kefir and Rhodococcus sp., which earlier turned out to be suitable for a chemoenzymatic one-pot synthesis with organocatalysts, were immobilized with their cofactors on a commercially available superabsorber based on a literature known protocol. The use of the immobilized ADH from L. kefir in the reduction of acetophenone as a model substrate led to high conversion (>95