Biochemical characterization of ethanol-dependent reduction of furfural by alcohol dehydrogenases

Qunrui Li; L K Metthew Lam; Luying Xun

doi:10.1007/s10532-011-9477-x

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Biochemical characterization of ethanol-dependent reduction of furfural by alcohol dehydrogenases

Journal article

Peer reviewed

Biochemical characterization of ethanol-dependent reduction of furfural by alcohol dehydrogenases

Qunrui Li, L K Metthew Lam and Luying Xun

Biodegradation (Dordrecht), Vol.22(6), pp.1227-1237

11/2011

DOI: https://doi.org/10.1007/s10532-011-9477-x

Handle:

https://hdl.handle.net/2376/105055

PMID: 21526389

Abstract

Furans - metabolism

Bacterial Proteins - chemistry

Molecular Sequence Data

Isoenzymes - chemistry

Phylogeny

Cupriavidus necator - genetics

Isoenzymes - isolation & purification

Recombinant Proteins - isolation & purification

Thermodynamics

Transformation, Bacterial

Isoenzymes - metabolism

Pseudomonas aeruginosa - enzymology

Alcohol Dehydrogenase - isolation & purification

Cloning, Molecular

Cupriavidus necator - enzymology

NAD - metabolism

Alcohol Dehydrogenase - chemistry

Alcohol Dehydrogenase - metabolism

Recombinant Proteins - metabolism

Amino Acid Sequence

Industrial Microbiology

Escherichia coli - enzymology

Ethanol - metabolism

Isoenzymes - genetics

Bacterial Proteins - genetics

Recombinant Proteins - chemistry

Recombinant Proteins - genetics

Furaldehyde - metabolism

Sequence Alignment

Pseudomonas aeruginosa - genetics

Escherichia coli - genetics

Plasmids

Alcohol Dehydrogenase - genetics

Saccharomyces cerevisiae - enzymology

Bacterial Proteins - metabolism

Kinetics

Bacterial Proteins - isolation & purification

Lignocellulosic biomass is usually converted to hydrolysates, which consist of sugars and sugar derivatives, such as furfural. Before yeast ferments sugars to ethanol, it reduces toxic furfural to non-inhibitory furfuryl alcohol in a prolonged lag phase. Bioreduction of furfural may shorten the lag phase. Cupriavidus necator JMP134 rapidly reduces furfural with a Zn-dependent alcohol dehydrogenase (FurX) at the expense of ethanol (Li et al. 2011). The mechanism of the ethanol-dependent reduction of furfural by FurX and three homologous alcohol dehydrogenases was investigated. The reduction consisted of two individual reactions: ethanol-dependent reduction of NAD(+) to NADH and then NADH-dependent reduction of furfural to furfuryl alcohol. The kinetic parameters of the coupled reaction and the individual reactions were determined for the four enzymes. The data indicated that limited NADH was released in the coupled reaction. The enzymes had high affinities for NADH (e.g., K ( d ) of 0.043 μM for the FurX-NADH complex) and relatively low affinities for NAD(+) (e.g., K ( d ) of 87 μM for FurX-NAD(+)). The kinetic data suggest that the four enzymes are efficient "furfural reductases" with either ethanol or NADH as the reducing power. The standard free energy change (ΔG°') for ethanol-dependent reduction of furfural was determined to be -1.1 kJ mol(-1). The physiological benefit for ethanol-dependent reduction of furfural is likely to replace toxic and recalcitrant furfural with less toxic and more biodegradable acetaldehyde.

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Title: Biochemical characterization of ethanol-dependent reduction of furfural by alcohol dehydrogenases
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.1227-1237
Academic Unit: Molecular Biosciences, School of
Publisher: Netherlands
Identifiers: 99900546929801842
Language: English
Resource Type: Journal article

Biochemical characterization of ethanol-dependent reduction of furfural by alcohol dehydrogenases

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