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Purification and characterization of a dimethoate-degrading enzyme of Aspergillus niger ZHY256, isolated from sewage. 2001
State Key Laboratory for Biocontrol, School of Life Science, Zhong Shan University, Guang Zhou 510275, People's Republic of China. Lsslyh@zsu.edu.cn
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 degrees 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 micromol min(-1) mg of protein(-1), respectively.
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