Cupriavidus necator JMP134 rapidly reduces furfural with a Zn-dependent alcohol dehydrogenase

Qunrui Li; L K Metthew Lam; Luying Xun

doi:10.1007/s10532-011-9476-y

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Cupriavidus necator JMP134 rapidly reduces furfural with a Zn-dependent alcohol dehydrogenase

Journal article

Peer reviewed

Cupriavidus necator JMP134 rapidly reduces furfural with a Zn-dependent alcohol dehydrogenase

Qunrui Li, L K Metthew Lam and Luying Xun

Biodegradation (Dordrecht), Vol.22(6), pp.1215-1225

11/2011

DOI: https://doi.org/10.1007/s10532-011-9476-y

Handle:

https://hdl.handle.net/2376/104999

PMID: 21526390

Abstract

Furans - metabolism

Zinc - metabolism

Bacterial Proteins - chemistry

Biomass

Cupriavidus necator - genetics

Recombinant Proteins - isolation & purification

Saccharomyces cerevisiae - metabolism

Lignin - metabolism

Transformation, Bacterial

Alcohol Dehydrogenase - isolation & purification

Cloning, Molecular

Cupriavidus necator - enzymology

NAD - metabolism

Alcohol Dehydrogenase - chemistry

Alcohol Dehydrogenase - metabolism

Recombinant Proteins - metabolism

Industrial Microbiology

Escherichia coli - enzymology

Ethanol - metabolism

Oxidation-Reduction

Bacterial Proteins - genetics

Recombinant Proteins - chemistry

Recombinant Proteins - genetics

Fermentation

Furaldehyde - metabolism

Escherichia coli - genetics

Plasmids

Alcohol Dehydrogenase - genetics

Bacterial Proteins - metabolism

Kinetics

Bacterial Proteins - isolation & purification

Ethanol is a renewable biofuel, and it can be produced from lignocellulosic biomass. The biomass is usually converted to hydrolysates that consist of sugar and sugar derivatives, such as furfural. Yeast ferments sugar to ethanol, but furfural higher than 3 mM is inhibitory. It can take several days for yeast cells to reduce furfural to non-inhibitory furfuryl alcohol before producing ethanol. Bioreduction of furfural to furfuryl alcohol before fermentation may relieve yeast from furfural toxicity. We observed that Cupriavidus necator JMP134, a strict aerobe, rapidly reduced 17 mM furfural to less than 3 mM within 14 min with cell turbidity of 1.0 at 600 nm at 50°C. The rapid reduction consumed ethanol. The "furfural reductase" (FurX) was purified, and it oxidized ethanol to acetaldehyde and reduced furfural to furfuryl alcohol with NAD(+) as the cofactor. The protein was identified with mass spectrometry fingerprinting to be a hypothetical protein belonging to Zn-dependent alcohol dehydrogenase family. The furX-inactivation mutant of C. necator JMP134 lost the ability to rapidly reduce furfural, and Escherichia coli producing recombinant FurX gained the ability. Thus, an alcohol dehydrogenase enabled bacteria to rapidly reduce furfural with ethanol as the reducing power.

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Title: Cupriavidus necator JMP134 rapidly reduces furfural with a Zn-dependent alcohol dehydrogenase
Creators: Qunrui Li - School of Molecular Biosciences, Washington State University, Life Sciences Building, Room 202, 100 Dairy Road, Pullman, WA 99164-7520, USA
L K Metthew Lam
Luying Xun
Publication Details: Biodegradation (Dordrecht), Vol.22(6), pp.1215-1225
Academic Unit: Molecular Biosciences, School of
Publisher: Netherlands
Identifiers: 99900547099401842
Language: English
Resource Type: Journal article

Cupriavidus necator JMP134 rapidly reduces furfural with a Zn-dependent alcohol dehydrogenase

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