Superabsorbed alcohol dehydrogenase—a new catalyst for asymmetric reductions |
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Authors: | Günter E Jeromin |
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Institution: | 1.Aachen University of Applied Sciences,Jülich,Germany |
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Abstract: | A new immobilisate of alcohol dehydrogenase (ADH) is described in which all components for the reaction, i.e. enzyme, the
coenzyme NADP+, the buffer and other cofactors (trace elements), are immobilized together. It is an all-inclusive catalyst. The support
is a cheap, commercially-available, superabsorbent polymer. The immobilisation is easy to achieve. The superabsorbed ADH is,
even when dried, a stable and storable catalyst for at least five weeks at −18°C. Asymmetric reductions of the prochiral ketones,
acetophenone, 4-acetylpyridine and ethyl acetoacetate, with a superabsorbed ADH from Lactobacillus brevis (ADH 002) and a superabsorbed ADH from Thermoanaerobicum sp. (ADH 005) in 2-propanol as both the organic solvent and the cofactor-regenerating substrate are given. Yields of chiral
(R) and (S)-alcohols from 97–100% were achieved within 18 to 48 h with enantiomeric excesses of >99%. The superabsorbed ADH was easily
separated by filtration and could be reused at least four times. |
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Keywords: | |
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