Purification and characterization of a novel carbaryl hydrolase from Aspergillus niger PY168

FEMS Microbiol Lett. 2003 Nov 7;228(1):39-44. doi: 10.1016/S0378-1097(03)00718-3.


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 pI of 4.6, and the enzyme activity was optimal at 45 degrees C and pH 7.5, The activities were strongly inhibited by Hg(2+), Ag+, rho-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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aspergillus niger / enzymology*
  • Carbaryl / metabolism*
  • Enzyme Activation / drug effects
  • Enzyme Inhibitors / pharmacology
  • Hydrogen-Ion Concentration
  • Hydrolases / isolation & purification
  • Hydrolases / metabolism*
  • Insecticides / metabolism*
  • Iodoacetic Acid / pharmacology
  • Metals / pharmacology
  • Substrate Specificity
  • Sulfhydryl Reagents / pharmacology
  • Temperature
  • p-Chloromercuribenzoic Acid / pharmacology


  • Enzyme Inhibitors
  • Insecticides
  • Metals
  • Sulfhydryl Reagents
  • p-Chloromercuribenzoic Acid
  • Hydrolases
  • Carbaryl
  • Iodoacetic Acid