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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  • Author(s): Gutiérrez T;Gutiérrez T; Ingram LO; Preston JF
  • Source:
    Journal of biotechnology [J Biotechnol] 2006 Jan 24; Vol. 121 (2), pp. 154-64. Date of Electronic Publication: 2005 Aug 18.
  • Publication Type:
    Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Elsevier Science Publishers Country of Publication: Netherlands NLM ID: 8411927 Publication Model: Print-Electronic Cited Medium: Print ISSN: 0168-1656 (Print) Linking ISSN: 01681656 NLM ISO Abbreviation: J Biotechnol Subsets: MEDLINE
    • Publication Information:
      Original Publication: Amsterdam : Elsevier Science Publishers, c1984-
    • Subject Terms:
      Aldehyde Reductase/*isolation & purification ; Bacterial Proteins/*isolation & purification ; Escherichia coli/*enzymology ; Ethanol/*metabolism ; Furaldehyde/*metabolism ; Oxidoreductases/*isolation & purification; Aldehyde Reductase/chemistry ; Aldehyde Reductase/metabolism ; Bacterial Proteins/chemistry ; Bacterial Proteins/metabolism ; Escherichia coli/genetics ; Oxidoreductases/chemistry ; Oxidoreductases/metabolism ; Substrate Specificity
    • 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 approximately 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 degrees C), and an apparent Km and Vmax for furfural of 1.5x10(-4)M and 28.5 micromol/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.
    • Accession Number:
      0 (Bacterial Proteins)
      3K9958V90M (Ethanol)
      DJ1HGI319P (Furaldehyde)
      EC 1.- (Oxidoreductases)
      EC 1.1.1.21 (Aldehyde Reductase)
      EC 1.1.1.21 (furfural reductase, E coli)
    • Publication Date:
      Date Created: 20050823 Date Completed: 20060621 Latest Revision: 20131121
    • Publication Date:
      20221213
    • Accession Number:
      10.1016/j.jbiotec.2005.07.003
    • Accession Number:
      16111779