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Superabsorbed alcohol dehydrogenase—a new catalyst for asymmetric reductions

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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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Acknowledgments

This work was supported by the Kompetenzplattform Bioengineering Jülich (KOPF), financed by the Ministry for Innovation, Science, Research and Technology of North-Rhine Westphalia (Ministerium für Innovation, Wissenschaft, Forschung und Technologie des Landes Nordrhein-Westfalen (MIWFT- NRW)), GC-analytics were made by Dr. Andrea Butzen from Julich Chiral Solutions GmbH and enzyme activities were produced by Robert Kuss of the Aachen University of Applied Sciences.

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  1. Aachen University of Applied Sciences, Campus Jülich, FB 3, Ginsterweg 1, 52428, Jülich, Germany

    Günter E. Jeromin

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  1. Günter E. Jeromin
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Correspondence to Günter E. Jeromin.

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Jeromin, G.E. Superabsorbed alcohol dehydrogenase—a new catalyst for asymmetric reductions. Biotechnol Lett 31, 1717–1721 (2009). https://doi.org/10.1007/s10529-009-0062-x

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  • DOI: https://doi.org/10.1007/s10529-009-0062-x

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