Purification and characterization of fenitrothion hydrolase from Burkholderia sp. NF100

J Biosci Bioeng. 2006 Jan;101(1):80-2. doi: 10.1263/jbb.101.80.

Abstract

The organophosphorus pesticide hydrolase was purified to homogeneity from Burkholderia sp. NF100 by detergent extraction of the cell membrane fraction, anion-exchange, chromatofocusing, and gel filtration chromatographies. The purified enzyme had a molecular mass of 55 kDa and a pI 5.8, and the hydrolase activity was strongly inhibited by EDTA, dithiothreitol (DTT), Hg2+ and 1,10-phenanthroline. The optimum pH and temperature for the enzyme activity were 8.0 and 40 degrees C, respectively. The enzyme hydrolyzed five organophosphorus pesticides.

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / isolation & purification
  • Burkholderia / enzymology*
  • Chromatography
  • Dithiothreitol / pharmacology
  • Edetic Acid / pharmacology
  • Fenitrothion / metabolism*
  • Hydrolases / antagonists & inhibitors
  • Hydrolases / chemistry*
  • Hydrolases / isolation & purification
  • Mercury / pharmacology
  • Molecular Weight
  • Pesticides / chemistry
  • Phenanthrolines / pharmacology

Substances

  • Bacterial Proteins
  • Pesticides
  • Phenanthrolines
  • Edetic Acid
  • Hydrolases
  • Mercury
  • Dithiothreitol
  • 1,10-phenanthroline
  • Fenitrothion