Purification and characterization of carbaryl hydrolase from Arthrobacter sp RC100

被引：28
作者：
Hayatsu, M
Mizutani, A
Hashimoto, M
Sato, K
Hayano, K
机构：
[1] Shizuoka Univ, Fac Agr, Shizuoka 4228529, Japan
[2] Biooriented Technol Res Advancement Inst, Minato Ku, Tokyo 1050001, Japan
来源：
FEMS MICROBIOLOGY LETTERS | 2001年 / 201卷 / 01期
关键词：
carbaryl; hydrolase; carbamate pesticide; Arthrobacter;
D O I：
10.1016/S0378-1097(01)00255-5
中图分类号：
Q93 [微生物学];
学科分类号：
071005 ; 100705 ;
摘要：
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 degreesC, respectively. The enzyme hydrolyzed four N-methylcarbamate insecticides (carbaryl, xylylcarb, metolcarb and XMC), but was not able to hydrolyze fenobucarb, propoxur, and isoprocarb. (C) 2001 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.
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页码：99 / 103
页数：5
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