Purification and characterization of a novel pyrethroid hydrolase from Aspergillus niger ZD11.
The pyrethroid pesticides residues on foods and environmental contamination are a public safety concern. Pretreatment with pyrethroid hydrolase has the potential to alleviate the conditions. For this purpose, a fungus capable of using pyrethroid pesticides as a sole carbon source was isolated from the soil and characterized as Aspergillus niger ZD11. A novel pyrethroid hydrolase from cell extract was purified 41.5-fold to apparent homogeneity with 12.6% overall recovery. It is a monomeric structure with a molecular mass of 56 kDa, a pI of 5.4, and the enzyme activity was optimal at 45 degrees C and pH 6.5. The activities were strongly inhibited by Hg(2+), Ag(+), and rho-chloromercuribenzoate, whereas less pronounced effects (5-10% inhibition) were observed in the presence of the remaining divalent cations, the chelating agent EDTA and phenanthroline. The purified enzyme hydrolyzed various insecticides with similar carboxylester. trans-Permethrin is the preferred substrate.
Liang
Wei Q
WQ
State Key Laboratory of Biocontrol, School of Life Science, Zhongshan University, Guangzhou, People's Republic of China.
Wang
Zhuo Y
ZY
Li
He
H
Wu
Pei C
PC
Hu
Ji M
JM
Luo
Na
N
Cao
Li X
LX
Liu
Yu H
YH
D001234:Aspergillus niger / Q000201:enzymology*; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D006867:Hydrolases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D008970:Molecular Weight; D011722:Pyrethrins / Q000378:metabolism*; D013379:Substrate Specificity; D013696:Temperature
D011722:Pyrethrins; D006867:Hydrolases