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• W2807224175 abstract "Abstract Full length open reading frame of pyrethroid detoxification gene, Est3385 , contains 963 nucleotides. This gene was identified and cloned based on the genome sequence of Rhodopseudomonas palustris PSB-S available at the GneBank. The predicted amino acid sequence of Est3385 shared moderate identities (30–46%) with the known homologous esterases. Phylogenetic analysis revealed that Est3385 was a member in the esterase family I. Recombinant Est3385 was heterologous expressed in E. coli , purified and characterized for its substrate specificity, kinetics and stability under various conditions. The optimal temperature and pH for Est3385 were 35 °C and 6.0, respectively. This enzyme could detoxify various pyrethroid pesticides and degrade the optimal substrate fenpropathrin with a K m and V max value of 0.734 ± 0.013 mmol·l −1 and 0.918 ± 0.025 U·µg −1 , respectively. No cofactor was found to affect Est3385 activity but substantial reduction of enzymatic activity was observed when metal ions were applied. Taken together, a new pyrethroid degradation esterase was identified and characterized. Modification of Est3385 with protein engineering toolsets should enhance its potential for field application to reduce the pesticide residue from agroecosystems." @default.
• W2807224175 created "2018-06-13" @default.
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• W2807224175 date "2018-05-09" @default.
• W2807224175 modified "2023-09-27" @default.
• W2807224175 title "Cloning and characterization of a pyrethroid pesticide decomposing esterase gene, Est3385, from Rhodopseudomonas palustris PSB-S" @default.
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• W2807224175 doi "https://doi.org/10.1038/s41598-018-25734-9" @default.
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