Dataset Information

Identification of a marine Bacillus strain C5 and parathion-methyl degradation characteristics of the extracellular esterase B1.

ABSTRACT: A bacterial strain C5 that can produce new type of marine esterase was isolated and screened from marine sludge. According to 16S rRNA sequence analysis and physiological and biochemical experiments, the strain was identified as Bacillus subtilis. A single isozyme with a molecular weight of 86?kDa was observed by SDS-PAGE and native-PAGE. On this basis, the mechanism of esterase B1 secreted by strain C5 degrading parathion-methyl was explored, and the effects of temperature and pH on the degradation rate were investigated. From the results, p-nitrophenol was one of the degradation products of B1 degrading parathion-methyl, and the best degradation effect could be achieved at the temperature of 40°C and the neutral pH value.

SUBMITTER: Hao J

PROVIDER: S-EPMC4279127 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature

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Identification of a marine Bacillus strain C5 and parathion-methyl degradation characteristics of the extracellular esterase B1.

Hao Jianhua J Liu Junzhong J Sun Mi M

BioMed research international 20141211

A bacterial strain C5 that can produce new type of marine esterase was isolated and screened from marine sludge. According to 16S rRNA sequence analysis and physiological and biochemical experiments, the strain was identified as Bacillus subtilis. A single isozyme with a molecular weight of 86 kDa was observed by SDS-PAGE and native-PAGE. On this basis, the mechanism of esterase B1 secreted by strain C5 degrading parathion-methyl was explored, and the effects of temperature and pH on the degrada ...[more]

PMID: 25580438

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Project description:Strobilurin fungicides are widely used in agricultural production due to their broad-spectrum and fungal mitochondrial inhibitory activities. However, their massive application has restrained the growth of eukaryotic algae and increased collateral damage in freshwater systems, notably harmful cyanobacterial blooms (HCBs). In this study, a strobilurin fungicide-degrading strain, Hyphomicrobium sp. strain DY-1, was isolated and characterized successfully. Moreover, a novel esterase gene, strH, responsible for the de-esterification of strobilurin fungicides, was cloned, and the enzymatic properties of StrH were studied. For trifloxystrobin, StrH displayed maximum activity at 50°C and pH 7.0. The catalytic efficiencies (kcat/Km ) of StrH for different strobilurin fungicides were 196.32 ± 2.30 μM-1 · s-1 (trifloxystrobin), 4.64 ± 0.05 μM-1 · s-1 (picoxystrobin), 2.94 ± 0.02 μM-1 · s-1 (pyraclostrobin), and (2.41 ± 0.19)×10-2 μM-1 · s-1 (azoxystrobin). StrH catalyzed the de-esterification of a variety of strobilurin fungicides, generating the corresponding parent acid to achieve the detoxification of strobilurin fungicides and relieve strobilurin fungicide growth inhibition of Chlorella This research will provide insight into the microbial remediation of strobilurin fungicide-contaminated environments.IMPORTANCE Strobilurin fungicides have been widely acknowledged as an essential group of pesticides worldwide. So far, their residues and toxic effects on aquatic organisms have been reported in different parts of the world. Microbial degradation can eliminate xenobiotics from the environment. Therefore, the degradation of strobilurin fungicides by microorganisms has also been reported. However, little is known about the involvement of enzymes or genes in strobilurin fungicide degradation. In this study, a novel esterase gene responsible for the detoxification of strobilurin fungicides, strH, was cloned in the newly isolated strain Hyphomicrobium sp. DY-1. This degradation process detoxifies the strobilurin fungicides and relieves their growth inhibition of Chlorella.

Dataset Information

Identification of a marine Bacillus strain C5 and parathion-methyl degradation characteristics of the extracellular esterase B1.

Publications

Identification of a marine Bacillus strain C5 and parathion-methyl degradation characteristics of the extracellular esterase B1.

Similar Datasets

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