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  • Title: Purification and characterization of carbaryl hydrolase from Arthrobacter sp. RC100.
    Author: Hayatsu M, Mizutani A, Hashimoto M, Sato K, Hayano K.
    Journal: FEMS Microbiol Lett; 2001 Jul 10; 201(1):99-103. PubMed ID: 11445174.
    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, 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.
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