Purification and characterization of a novel organophosphorus pesticide hydrolase from Penicillium lilacinum BP303
Enzyme and Microbial Technology(2004)
Abstract
A Penicillium lilacinum BP303 was found to be able to degrade various organophosphorus pesticides by cleaving PO in the phosphotriesters bond and PS linkage in the phosphothiolesters effectively. The novel fungal enzyme hydrolyzing methyl parathion, parathion, paraoxon, coumaphos, demeton-S, phosmet, and malathion has been purified to homogeneity and characterized. It is a monomeric structure with a molecular mass of 60,000Da, a pI of 4.8, and the enzyme activity was optimal at 45°C and pH 7.5, The activities were strongly inhibited by Hg2+, Fe3+, ρ-chloromercuribenzoate, iodoacetic acid, and N-ethylmaleimide, while Cu2+, β-mercaptoethanol, dithiothreitol, dithioerythritol, glutathione, and detergents slightly activated the enzyme. As judged by catalytic efficiencies, paraoxon is the preferred substrate.
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Key words
Organophosphorus pesticide hydrolyzing enzyme,Penicillium lilacinum,Purification,Properties
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