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Applied and Environmental Microbiology, August 2001, p. 3746-3749, Vol. 67, No. 8
0099-2240/01/$04.00+0   DOI: 10.1128/AEM.67.8.3746-3749.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

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

Yu-Huan Liu,1,* Ying-Cheng Chung,1 and Ya Xiong2

State Key Laboratory for Biocontrol, School of Life Science,1 and School of Chemistry and Chemical Engineering,2 Zhong Shan University, Guang Zhou 510275, People's Republic of China

Received 8 January 2001/Accepted 9 May 2001

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 Cu2+. The Michaelis constant (Km) and Vmax for dimethoate were 1.25 mM and 292 µmol min-1 mg of protein-1, respectively.

* Corresponding author. Mailing address: School of Life Science, Zhong Shan University, Guang Zhou 510275, People's Republic of China. Phone: 020-84110786. Fax: 020-84036215. E-mail: Lsslyh{at}zsu.edu.cn.

Applied and Environmental Microbiology, August 2001, p. 3746-3749, Vol. 67, No. 8
0099-2240/01/$04.00+0   DOI: 10.1128/AEM.67.8.3746-3749.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.




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