Open AccessPurification and characterization of a novel carbaryl hydrolase from Aspergillus niger PY168
Author(s) -
Qing Zhang,
Yang Liu,
YuHuan Liu
Publication year - 2003
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1016/s0378-1097(03)00718-3
Subject(s) - carbaryl , phenylmethylsulfonyl fluoride , hydrolase , aspergillus niger , chemistry , hydrolysis , chromatography , enzyme , biochemistry , specific activity , nuclear chemistry , stereochemistry , biology , protease , pesticide , agronomy
A fungus capable of using carbaryl as the sole source of carbon and energy was isolated from a soil enrichment, and characterized as Aspergillus niger and designated strain PY168. A novel carbaryl hydrolase from cell extract was purified 262‐fold to apparent homogeneity with 13.6% overall recovery. It had a monomeric structure with a molecular mass of 50 000 Da and a p I of 4.6, and the enzyme activity was optimal at 45°C and pH 7.5, The activities were strongly inhibited by Hg 2+ , Ag + , ρ‐chloromercuribenzoate, iodoacetic acid, diisofluorophosphate and phenylmethylsulfonyl fluoride but not EDTA and phenanthroline. The purified enzyme hydrolyzed various N ‐methylcarbamate insecticides. Carbaryl is the preferred substrate.