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Cloning and characterization of a pyrethroid pesticide decomposing esterase gene, Est3385, from Rhodopseudomonas palustris PSB-S
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...
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Published in: | Scientific reports 2018-05, Vol.8 (1), p.7384-8, Article 7384 |
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Main Authors: | , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | 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. |
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ISSN: | 2045-2322 2045-2322 |
DOI: | 10.1038/s41598-018-25734-9 |