Purification and characterization of fenitrothion hydrolase from Burkholderia sp. NF100.
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.
Tago
Kanako
K
United Graduate School of Agricultural Science, Gifu University, 1-1 Yanagido, Gifu City, Gifu 501-1193, Japan.
Yonezawa
Sumiko
S
Ohkouchi
Toshihide
T
Hashimoto
Masayuki
M
Hayatsu
Masahito
M
D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification; D019117:Burkholderia / Q000201:enzymology*; D002845:Chromatography; D004229:Dithiothreitol / Q000494:pharmacology; D004492:Edetic Acid / Q000494:pharmacology; D005278:Fenitrothion / Q000378:metabolism*; D006867:Hydrolases / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000302:isolation & purification; D008628:Mercury / Q000494:pharmacology; D008970:Molecular Weight; D010575:Pesticides / Q000737:chemistry; D010618:Phenanthrolines / Q000494:pharmacology
D001426:Bacterial Proteins; D010575:Pesticides; D010618:Phenanthrolines; D004492:Edetic Acid; D006867:Hydrolases; D008628:Mercury; D004229:Dithiothreitol; C025205:1,10-phenanthroline; D005278:Fenitrothion