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 language | English |
|---|---|
| Pages (from-to) | 80-82 |
| Number of pages | 3 |
| Journal | Journal of Bioscience and Bioengineering |
| Volume | 101 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - 2006 Jan 1 |
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All Science Journal Classification (ASJC) codes
- Biotechnology
- Bioengineering
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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 journal › Article
TY - JOUR
T1 - Purification and characterization of fenitrothion hydrolase from Burkholderia sp. NF100
AU - Tago, Kanako
AU - Yonezawa, Sumiko
AU - Ohkouchi, Toshihide
AU - Hashimoto, Masayuki
AU - Hayatsu, Masahito
PY - 2006/1/1
Y1 - 2006/1/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=33646261874&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=33646261874&partnerID=8YFLogxK
U2 - 10.1263/jbb.101.80
DO - 10.1263/jbb.101.80
M3 - Article
VL - 101
SP - 80
EP - 82
JO - Journal of Bioscience and Bioengineering
JF - Journal of Bioscience and Bioengineering
SN - 1389-1723
IS - 1
ER -