Purification and characterization of carbaryl hydrolase from Arthrobacter sp. RC100

Masahito Hayatsu, Atushi Mizutani, Masayuki Hashimoto, Koji Sato, Koichi Hayano

研究成果: Article同行評審

40 引文 斯高帕斯(Scopus)

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°C, respectively. The enzyme hydrolyzed four N-methylcarbamate insecticides (carbaryl, xylylcarb, metolcarb and XMC), but was not able to hydrolyze fenobucarb, propoxur, and isoprocarb.

原文English
頁(從 - 到)99-103
頁數5
期刊FEMS Microbiology Letters
201
發行號1
DOIs
出版狀態Published - 2001 7月 10

All Science Journal Classification (ASJC) codes

  • 微生物學
  • 分子生物學
  • 遺傳學

指紋

深入研究「Purification and characterization of carbaryl hydrolase from Arthrobacter sp. RC100」主題。共同形成了獨特的指紋。

引用此