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
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Bacterial Proteins / chemistry*
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Bacterial Proteins / isolation & purification
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Burkholderia / enzymology*
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Chromatography
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Dithiothreitol / pharmacology
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Edetic Acid / pharmacology
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Fenitrothion / metabolism*
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Hydrolases / antagonists & inhibitors
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Hydrolases / chemistry*
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Hydrolases / isolation & purification
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Mercury / pharmacology
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Molecular Weight
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Pesticides / chemistry
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Phenanthrolines / pharmacology
Substances
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Bacterial Proteins
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Pesticides
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Phenanthrolines
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Edetic Acid
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Hydrolases
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Mercury
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Dithiothreitol
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1,10-phenanthroline
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Fenitrothion