Purification and Characterization of a Dimethoate-Degrading Enzyme of Aspergillus niger ZHY256, Isolated from Sewage

Author:

Liu Yu-Huan1,Chung Ying-Cheng1,Xiong Ya2

Affiliation:

1. State Key Laboratory for Biocontrol, School of Life Science,1 and

2. School of Chemistry and Chemical Engineering,2 Zhong Shan University, Guang Zhou 510275, People's Republic of China

Abstract

ABSTRACT A dimethoate-degrading enzyme from Aspergillus niger ZHY256 was purified to homogeneity with a specific activity of 227.6 U/mg of protein. The molecular mass of the purified enzyme was estimated to be 66 kDa by gel filtration and 67 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The isoelectric point was found to be 5.4, and the enzyme activity was optimal at 50°C and pH 7.0. The activity was inhibited by most of the metal ions and reagents, while it was induced by Cu 2+ . The Michaelis constant ( K m ) and V max for dimethoate were 1.25 mM and 292 μmol min −1 mg of protein −1 , respectively.

Publisher

American Society for Microbiology

Subject

Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology

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