<Emphasis Type="Italic">Cupriavidus necator</Emphasis> JMP134 rapidly reduces furfural with a Zn-dependent alcohol dehydrogenase |
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Authors: | Qunrui Li L K Metthew Lam Luying Xun |
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Institution: | (1) School of Molecular Biosciences, Washington State University, Life Sciences Building, Room 202, 100 Dairy Road, Pullman, WA 99164-7520, USA; |
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Abstract: | 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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