Purification and characterization of fenitrothion hydrolase from Burkholderia sp. NF100.
J Biosci Bioeng
; 101(1): 80-2, 2006 Jan.
Article
en En
| MEDLINE
| ID: mdl-16503297
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.
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Banco de datos:
MEDLINE
Asunto principal:
Proteínas Bacterianas
/
Burkholderia
/
Fenitrotión
/
Hidrolasas
Idioma:
En
Año:
2006
Tipo del documento:
Article