Purification and characterization of fenitrothion hydrolase from Burkholderia sp. NF100

Kanako Tago, Sumiko Yonezawa, Toshihide Ohkouchi, Masayuki Hashimoto, Masahito Hayatsu

Research output: Contribution to journalArticlepeer-review

18 Citations (Scopus)


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°C, respectively. The enzyme hydrolyzed five organophosphorus pesticides.

Original languageEnglish
Pages (from-to)80-82
Number of pages3
JournalJournal of Bioscience and Bioengineering
Issue number1
Publication statusPublished - 2006 Jan

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology


Dive into the research topics of 'Purification and characterization of fenitrothion hydrolase from Burkholderia sp. NF100'. Together they form a unique fingerprint.

Cite this