Purification and characterization of fenitrothion hydrolase from Burkholderia sp. NF100 |
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| Authors: | Tago Kanako Yonezawa Sumiko Ohkouchi Toshihide Hashimoto Masayuki Hayatsu Masahito |
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| Affiliation: | United Graduate School of Agricultural Science, Gifu University, 1-1 Yanagido, Gifu City, Gifu 501-1193, Japan. |
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| 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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