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Horse liver alcohol dehydrogenase coimmobilized

Fig. 7. Horse-liver alcohol dehydrogenase (HLADH) catalyzed alcohol oxidation at a graphite felt anode modified by poly(acrylic acid) (PAA) under coimmobilization of ferrocene derivatives (Fc), diaphorase (Dp), and HLADH [39]... Fig. 7. Horse-liver alcohol dehydrogenase (HLADH) catalyzed alcohol oxidation at a graphite felt anode modified by poly(acrylic acid) (PAA) under coimmobilization of ferrocene derivatives (Fc), diaphorase (Dp), and HLADH [39]...
The use of enzymes for the enantioselective oxidation of prochiral (or racemic) diols has proved to be of significant synthetic interest. A range of simple racemic 1,2-diols proved to be good substrates for a system involving coimmobilized horse liver alcohol dehydrogenase (HLADH) and aldehyde dehydrogenase (AldDH) with NAD cofactor recycling. This produced enantiomerically pure a-hydroxycarbox-ylic acids (Scheme 12). [Pg.316]

See other pages where Horse liver alcohol dehydrogenase coimmobilized is mentioned: [Pg.109]    [Pg.1111]    [Pg.316]    [Pg.101]   


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Alcohol dehydrogenases

Alcohol liver

Coimmobilization

Dehydrogenases alcohol dehydrogenase

Horse

Horse alcohol dehydrogenases

Horse liver

Horse liver alcohol

Horse liver alcohol dehydrogenase

Horse liver alcohol dehydrogenases

Liver alcoholics

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