Purification and characterization of carbaryl hydrolase from Arthrobacter sp RC100

A carbaryl hydrolase was purified to homogeneity from Arthrobacter sp. stra in RC100 by protamine sulfate: treatment, ammonium sulfate precipitation, a nd hydrophobic. anion-exchange, and gel filtration chromatographies. The na tive enzyme had a molecular mass of 100 kDa and was composed of two identic al subunits with molecular masses of 51 kDa. The hydrolase activity was str ongly inhibited by DIFP, PMSF. Hg2+ and paraoxon but not by EDTA. The optim um pH and temperature for the enzyme activity were 9.0 and 50 degreesC, res pectively. The enzyme hydrolyzed four N-methylcarbamate insecticides (carba ryl, xylylcarb, metolcarb and XMC), but was not able to hydrolyze fenobucar b, propoxur, and isoprocarb. (C) 2001 Federation of European Microbiologica l Societies. Published by Elsevier Science B.V. All rights reserved.