Purification and characterization of carbaryl hydrolase from Arthrobacter sp. RC100

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

Research output: Contribution to journalArticlepeer-review

40 Citations (Scopus)

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, 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.

Original languageEnglish
Pages (from-to)99-103
Number of pages5
JournalFEMS Microbiology Letters
Volume201
Issue number1
DOIs
Publication statusPublished - 2001 Jul 10

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Molecular Biology
  • Genetics

Fingerprint

Dive into the research topics of 'Purification and characterization of carbaryl hydrolase from Arthrobacter sp. RC100'. Together they form a unique fingerprint.

Cite this