Isolation and characterization of a 4-nitrotoluene-oxidizing enzyme from activated sludge by a metagenomic approach

Microbes Environ. 2010;25(2):133-9. doi: 10.1264/jsme2.me10110.

Abstract

To isolate a biocatalytic enzyme, metagenomic libraries were constructed in fosmids from samples of activated sludge used to treat coke plant wastewater. Six indigo-producing clones were isolated from approximately 40,000 metagenomic clones in the search for the oxygenase responsible. In vitro mutagenesis and whole-sequencing revealed one open reading frame to be responsible for the production of indigo in the fosmid clones. The deduced sequence of the gene product showed 60% identity with 2-naphthoate monooxygenase from Burkholderia sp. JT1500. Subclones carrying this open reading frame (icpA) retained indigo production, and indigo-producing enzymes expressed from subclones catalyzed the oxidization of 4-nitrotoluene to form 4-nitrobenzyl alcohol. These results suggested that the icp product is an enzyme involved in catalyzing 4-nitrotoluene's oxygenation.

MeSH terms

  • Base Sequence
  • Benzyl Alcohols / metabolism
  • Catalysis
  • Cloning, Molecular
  • DNA / chemistry
  • DNA / genetics
  • DNA / isolation & purification
  • Escherichia coli / enzymology
  • Escherichia coli / genetics
  • Genomic Library
  • Industrial Waste*
  • Japan
  • Metagenomics / methods*
  • Mixed Function Oxygenases / genetics
  • Mixed Function Oxygenases / metabolism*
  • Molecular Sequence Data
  • Mutagenesis, Insertional
  • Open Reading Frames / genetics
  • Oxidation-Reduction
  • Sequence Analysis, DNA
  • Toluene / analogs & derivatives*
  • Toluene / metabolism

Substances

  • Benzyl Alcohols
  • Industrial Waste
  • Toluene
  • 4-nitrobenzyl alcohol
  • DNA
  • 4-nitrotoluene
  • Mixed Function Oxygenases

Associated data

  • GENBANK/AB362368
  • GENBANK/AB362369