TY - JOUR
T1 - Purification and characterization of carbaryl hydrolase from Arthrobacter sp. RC100
AU - Hayatsu, Masahito
AU - Mizutani, Atushi
AU - Hashimoto, Masayuki
AU - Sato, Koji
AU - Hayano, Koichi
N1 - Funding Information:
This work was supported by a program for the promotion of basic research activities for innovative biosciences of the Bio-oriented Technology Research Advancement Institution (Japan).
PY - 2001/7/10
Y1 - 2001/7/10
N2 - A carbaryl hydrolase was purified to homogeneity from Arthrobacter sp. strain RC100 by protamine sulfate treatment, ammonium sulfate precipitation, and hydrophobic, anion-exchange, and gel filtration chromatographies. The native enzyme had a molecular mass of 100 kDa and was composed of two identical subunits with molecular masses of 51 kDa. The hydrolase activity was strongly inhibited by DIFP, PMSF, Hg2+ and paraoxon but not by EDTA. The optimum pH and temperature for the enzyme activity were 9.0 and 50°C, respectively. The enzyme hydrolyzed four N-methylcarbamate insecticides (carbaryl, xylylcarb, metolcarb and XMC), but was not able to hydrolyze fenobucarb, propoxur, and isoprocarb.
AB - A carbaryl hydrolase was purified to homogeneity from Arthrobacter sp. strain RC100 by protamine sulfate treatment, ammonium sulfate precipitation, and hydrophobic, anion-exchange, and gel filtration chromatographies. The native enzyme had a molecular mass of 100 kDa and was composed of two identical subunits with molecular masses of 51 kDa. The hydrolase activity was strongly inhibited by DIFP, PMSF, Hg2+ and paraoxon but not by EDTA. The optimum pH and temperature for the enzyme activity were 9.0 and 50°C, respectively. The enzyme hydrolyzed four N-methylcarbamate insecticides (carbaryl, xylylcarb, metolcarb and XMC), but was not able to hydrolyze fenobucarb, propoxur, and isoprocarb.
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U2 - 10.1016/S0378-1097(01)00255-5
DO - 10.1016/S0378-1097(01)00255-5
M3 - Article
C2 - 11445174
AN - SCOPUS:0035838556
SN - 0378-1097
VL - 201
SP - 99
EP - 103
JO - FEMS Microbiology Letters
JF - FEMS Microbiology Letters
IS - 1
ER -