Aldehyde dehydrogenase coimmobilized

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). 

Wong and Matos (1985) reported a stereospecific oxidation of 1,2--diols to a-hydroxy carboxylic acids via a-hydroxy aldehydes.. The trick employed here is to coimmobilize HLADH and aldehyde dehydrogenase (AldDH) into polyacrylamide. The former enzyme oxidizes the diol to the corresponding a-hydroxy aldehyde, which is further oxidized to the a-hydroxy carboxylic acid by the latter enzyme (Scheme 34). After 40 % conversion of the substrates, enantiomer... 

Wong CH, Matos JR (1985) Enantioselective oxidation of 1,2-diols to L-a-hydroxy acids using coimmobilized alcohol and aldehyde dehydrogenase as catalysts. J Org Chem 50 1992-1994 Yasui S, Nakamura K, Ohno A, Oka S (1982) Reduction by a model of NAD(P)H. 36. First and direct evidence for the multi-step mechanism. Bull Chem Soc Jpn 55 196-199 Yasui S, Nakamura K, Ohno A (1983) Reduction by a model of NAD(P)H. 42. Direct evidence for one electron transfer mechanism in the reduction of arenediazonium salts. Tetrahedron Lett 24 3331-3334 Yasui S, Nakamura K, Ohno A (1984) Reduction by a model of NAD(P)H. 45. Mechanism for the dediazonation of arenediazonium salts initiated by one-electron transfer from an NAD(P)H-model. J Org Chem 49 878-882... 

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