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Purification and characterization of carbaryl hydrolase from Arthrobacter sp. RC100.

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, Hg(2+) and paraoxon but not by EDTA. The optimum pH and temperature for the enzyme activity were 9.0 and 50 degrees C, respectively. The enzyme hydrolyzed four N-methylcarbamate insecticides (carbaryl, xylylcarb, metolcarb and XMC), but was not able to hydrolyze fenobucarb, propoxur, and isoprocarb.[1]


  1. Purification and characterization of carbaryl hydrolase from Arthrobacter sp. RC100. Hayatsu, M., Mizutani, A., Hashimoto, M., Sato, K., Hayano, K. FEMS Microbiol. Lett. (2001) [Pubmed]
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