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Masahito Hayatsu, Atushi Mizutani, Masayuki Hashimoto, Koji Sato, Koichi Hayano, Purification and characterization of carbaryl hydrolase from Arthrobacter sp. RC100, FEMS Microbiology Letters, Volume 201, Issue 1, July 2001, Pages 99–103, https://doi.org/10.1111/j.1574-6968.2001.tb10739.x
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Abstract
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.