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Purification and characterization of a furfural reductase (FFR) from Escherichia coli strain LYO1—An enzyme important in the detoxification of furfural during ethanol production

Paper ID Volume ID Publish Year Pages File Format Full-Text
25728 43594 2006 11 PDF Available
Title
Purification and characterization of a furfural reductase (FFR) from Escherichia coli strain LYO1—An enzyme important in the detoxification of furfural during ethanol production
Abstract

Furfural, an inhibitor of ethanol production from hemicellulose acid hydrolysates, is reductively detoxified to furfuryl alcohol by the ethanologenic bacterium Escherichia coli strain LYO1. Furfural reductase was purified 106-fold from this bacterium to approximately 50% homogeneity. It has a native molecular mass of 135 kDa, determined by gel filtration, and subunit molecular mass of ∼68 kDa, determined by denaturing gel electrophoresis, indicating the holoenzyme is a dimer of two similar if not identical subunits. The enzyme shows strong activity from pH 4 to 8 (optimum pH 7.0), relatively high temperature tolerance (50–55 °C), and an apparent Km and Vmax for furfural of 1.5 × 10−4 M and 28.5 μmol/min/mg of protein, respectively. It catalyzes the essentially irreversible reduction of furfural with NADPH, is specific for NADPH as cofactor, and is relatively specific for the reduction of furfural and benzaldehyde; 2-acetylfuran, xylose, and glucose were not reduced, while acetaldehyde was reduced at a rate 25-fold lower than furfural. This is the first description of a furfural reductase which, based upon size and substrate specificity, appears to represent a new type of alcohol–aldehyde oxido-reductase. The conversion of relatively toxic furfural to less toxic furfuryl alcohol suggests a beneficial role for this enzyme in mitigating furfural toxicity encountered during ethanol production from lignocellulosic biomass.

Keywords
Furfural reductase (FFR); Furfural reduction; Furfuryl alcohol; Escherichia coli
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Purification and characterization of a furfural reductase (FFR) from Escherichia coli strain LYO1—An enzyme important in the detoxification of furfural during ethanol production
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 121, Issue 2, 24 January 2006, Pages 154–164
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us