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• W2115921622 endingPage "303" @default.
• W2115921622 startingPage "297" @default.
• W2115921622 abstract "A Penicillium lilacinum BP303 was found to be able to degrade various organophosphorus pesticides by cleaving PO in the phosphotriesters bond and PS 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 60,000 Da, 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." @default.
• W2115921622 created "2016-06-24" @default.
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• W2115921622 date "2004-03-01" @default.
• W2115921622 modified "2023-10-10" @default.
• W2115921622 title "Purification and characterization of a novel organophosphorus pesticide hydrolase from Penicillium lilacinum BP303" @default.
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• W2115921622 doi "https://doi.org/10.1016/j.enzmictec.2003.11.009" @default.
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