Purification and characterization of fenitrothion hydrolase from Burkholderia sp. NF100

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

Research output: Contribution to journalArticle

11 Citations (Scopus)

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

Original languageEnglish
Pages (from-to)80-82
Number of pages3
JournalJournal of Bioscience and Bioengineering
Volume101
Issue number1
DOIs
Publication statusPublished - 2006 Jan 1

Fingerprint

Fenitrothion
Burkholderia
Hydrolases
Pesticides
Purification
Enzymes
Dithiothreitol
Ethylenediaminetetraacetic acid
Detergents
Enzyme activity
Molecular mass
Cell membranes
Chromatography
Edetic Acid
Anions
Aryldialkylphosphatase
Ion exchange
Negative ions
Gels
Gel Chromatography

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Bioengineering

Cite this

Tago, Kanako ; Yonezawa, Sumiko ; Ohkouchi, Toshihide ; Hashimoto, Masayuki ; Hayatsu, Masahito. / Purification and characterization of fenitrothion hydrolase from Burkholderia sp. NF100. In: Journal of Bioscience and Bioengineering. 2006 ; Vol. 101, No. 1. pp. 80-82.
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Purification and characterization of fenitrothion hydrolase from Burkholderia sp. NF100. / Tago, Kanako; Yonezawa, Sumiko; Ohkouchi, Toshihide; Hashimoto, Masayuki; Hayatsu, Masahito.

In: Journal of Bioscience and Bioengineering, Vol. 101, No. 1, 01.01.2006, p. 80-82.

Research output: Contribution to journalArticle

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AU - Hayatsu, Masahito

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