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Identification of a Marine Bacillus Strain C5 and Parathion-Methyl Degradation Characteristics of the Extracellular Esterase B1

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 w...

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Detalles Bibliográficos
Autores principales: Hao, Jianhua, Liu, Junzhong, Sun, Mi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4279127/
https://www.ncbi.nlm.nih.gov/pubmed/25580438
http://dx.doi.org/10.1155/2014/863094
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author Hao, Jianhua
Liu, Junzhong
Sun, Mi
author_facet Hao, Jianhua
Liu, Junzhong
Sun, Mi
author_sort Hao, Jianhua
collection PubMed
description 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.
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spelling pubmed-42791272015-01-11 Identification of a Marine Bacillus Strain C5 and Parathion-Methyl Degradation Characteristics of the Extracellular Esterase B1 Hao, Jianhua Liu, Junzhong Sun, Mi Biomed Res Int Research Article 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. Hindawi Publishing Corporation 2014 2014-12-11 /pmc/articles/PMC4279127/ /pubmed/25580438 http://dx.doi.org/10.1155/2014/863094 Text en Copyright © 2014 Jianhua Hao et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Hao, Jianhua
Liu, Junzhong
Sun, Mi
Identification of a Marine Bacillus Strain C5 and Parathion-Methyl Degradation Characteristics of the Extracellular Esterase B1
title Identification of a Marine Bacillus Strain C5 and Parathion-Methyl Degradation Characteristics of the Extracellular Esterase B1
title_full Identification of a Marine Bacillus Strain C5 and Parathion-Methyl Degradation Characteristics of the Extracellular Esterase B1
title_fullStr Identification of a Marine Bacillus Strain C5 and Parathion-Methyl Degradation Characteristics of the Extracellular Esterase B1
title_full_unstemmed Identification of a Marine Bacillus Strain C5 and Parathion-Methyl Degradation Characteristics of the Extracellular Esterase B1
title_short Identification of a Marine Bacillus Strain C5 and Parathion-Methyl Degradation Characteristics of the Extracellular Esterase B1
title_sort identification of a marine bacillus strain c5 and parathion-methyl degradation characteristics of the extracellular esterase b1
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4279127/
https://www.ncbi.nlm.nih.gov/pubmed/25580438
http://dx.doi.org/10.1155/2014/863094
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