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Coupled oxidation–reduction of butanol–hexanal by resting Rhodococcus erythropolis NCIMB 13064 cells in liquid and gas phases

Marchand, Pierre and Rosenfeld, Eric and Erable, Benjamin and Maugard, Thierry and Lamare, Sylvain and Goubet, Isabelle Coupled oxidation–reduction of butanol–hexanal by resting Rhodococcus erythropolis NCIMB 13064 cells in liquid and gas phases. (2008) Enzyme and Microbial Technology, 43 (6). 423-430. ISSN 0141-0229

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Official URL: http://dx.doi.org/10.1016/j.enzmictec.2008.07.004


Rhodococcus erythropolis is a promising Gram-positive bacterium capable of numerous bioconversions including those involving alcohol dehydrogenases (ADHs). In this work, we compared and optimized the redox biocatalytic performances of 1-butanol-grown R. erythropolis NCIMB 13064 cells in aqueous and in non-conventional gas phase using the 1-butanol–hexanal oxidation–reduction as model reaction. Oxidation of 1-butanol to butanal is tightly coupled to the reduction of hexanal to 1-hexanol at the level of a nicotinoprotein–ADH-like enzyme. Cell viability is dispensable for reaction. In aqueous batch conditions, fresh and lyophilized cells are efficient redox catalysts (oxidation–reduction rate = 76 micromol min−1 g cell dry mass−1) being also reactive towards benzyl alcohol, (S)-2-pentanol, and geraniol as reductants. However, butanol hexanal oxidation–reduction is strongly limited by product accumulation and by hexanal toxicity that is amajor factor influencing cell behavior and performance. Reaction rate is maximal at 40 ◦C pH 7.0 in aqueous phase and at 60 ◦C- pH 7.0–9.0 in gas phase. Importantly, lyophilized cells also showed to be promising redox catalysts in the gas phase (at least 65 micromol min−1 g cell dry mass−1). The system is notably stable for several days at moderate thermodynamic activities of hexanal (0.06–0.12), 1-butanol (0.12) and water (0.7).

Item Type:Article
Additional Information:Thanks to Elsevier editor. The definitive version is available at http://www.sciencedirect.com The original PDF of the article can be found at Enzyme and Microbial Technology website : http://dx.doi.org/10.1016/j.enzmictec.2008.07.004
HAL Id:hal-04285316
Audience (journal):International peer-reviewed journal
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Institution:French research institutions > Centre National de la Recherche Scientifique - CNRS (FRANCE)
Other partners > Université de La Rochelle (FRANCE)
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Deposited On:17 Dec 2012 16:08

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