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Identification and enzymatic characterization of acid phosphatase from Burkholderia gladioli
BACKGROUND: The genus Burkholderia is widespread in diverse ecological niches, the majority of known species are soil bacteria that exhibit different types of non-pathogenic interactions with plants. Burkholderia species are versatile organisms that solubilize insoluble minerals through the producti...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3983855/ https://www.ncbi.nlm.nih.gov/pubmed/24713147 http://dx.doi.org/10.1186/1756-0500-7-221 |
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author | Rombola, Tiago Henrique Pedrinho, Eliamar Aparecida Nascimbem de Macedo Lemos, Eliana Gertrudes Gonçalves, Adriano Marques dos Santos, Luiz Flávio José Pizauro, João Martins |
author_facet | Rombola, Tiago Henrique Pedrinho, Eliamar Aparecida Nascimbem de Macedo Lemos, Eliana Gertrudes Gonçalves, Adriano Marques dos Santos, Luiz Flávio José Pizauro, João Martins |
author_sort | Rombola, Tiago Henrique |
collection | PubMed |
description | BACKGROUND: The genus Burkholderia is widespread in diverse ecological niches, the majority of known species are soil bacteria that exhibit different types of non-pathogenic interactions with plants. Burkholderia species are versatile organisms that solubilize insoluble minerals through the production of organic acids, which increase the availability of nutrients for the plant. Therefore these bacteria are promising candidates for biotechnological applications. RESULTS: Burkholderia sp. (R 3.25 isolate) was isolated from agricultural soil in Ponta Grossa-PR-Brazil and identified through analysis of the 16S rDNA as a strain classified as Burkholderia gladioli. The expression of membrane-bound acid phosphatase (MBAcP) was strictly regulated with optimal expression at a concentration of phosphorus 5 mM. The apparent optimum pH for the hydrolysis of p-nitrophenylphosphate (PNPP) was 6.0. The hydrolysis of PNPP by the enzyme exhibited a hyperbolic relationship with increasing concentration of substrate and no inhibition by excess of substrate was observed. Kinetic data revealed that the hydrolysis of PNPP exhibited cooperative kinetics with n = 1.3, V(m) = 113.5 U/mg and K(0.5) = 65 μM. The PNPPase activity was inhibited by vanadate, p-hydroxymercuribenzoate, arsenate and phosphate, however the activity was not inhibited by calcium, levamisole, sodium tartrate, EDTA, zinc, magnesium, cobalt, ouabain, oligomycin or pantoprazol. CONCLUSION: The synthesis of membrane-bound non-specific acid phosphatase, strictly regulated by phosphate, and its properties suggest that this bacterium has a potential biotechnological application to solubilize phosphate in soils with low levels of this element, for specific crops. |
format | Online Article Text |
id | pubmed-3983855 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-39838552014-04-12 Identification and enzymatic characterization of acid phosphatase from Burkholderia gladioli Rombola, Tiago Henrique Pedrinho, Eliamar Aparecida Nascimbem de Macedo Lemos, Eliana Gertrudes Gonçalves, Adriano Marques dos Santos, Luiz Flávio José Pizauro, João Martins BMC Res Notes Research Article BACKGROUND: The genus Burkholderia is widespread in diverse ecological niches, the majority of known species are soil bacteria that exhibit different types of non-pathogenic interactions with plants. Burkholderia species are versatile organisms that solubilize insoluble minerals through the production of organic acids, which increase the availability of nutrients for the plant. Therefore these bacteria are promising candidates for biotechnological applications. RESULTS: Burkholderia sp. (R 3.25 isolate) was isolated from agricultural soil in Ponta Grossa-PR-Brazil and identified through analysis of the 16S rDNA as a strain classified as Burkholderia gladioli. The expression of membrane-bound acid phosphatase (MBAcP) was strictly regulated with optimal expression at a concentration of phosphorus 5 mM. The apparent optimum pH for the hydrolysis of p-nitrophenylphosphate (PNPP) was 6.0. The hydrolysis of PNPP by the enzyme exhibited a hyperbolic relationship with increasing concentration of substrate and no inhibition by excess of substrate was observed. Kinetic data revealed that the hydrolysis of PNPP exhibited cooperative kinetics with n = 1.3, V(m) = 113.5 U/mg and K(0.5) = 65 μM. The PNPPase activity was inhibited by vanadate, p-hydroxymercuribenzoate, arsenate and phosphate, however the activity was not inhibited by calcium, levamisole, sodium tartrate, EDTA, zinc, magnesium, cobalt, ouabain, oligomycin or pantoprazol. CONCLUSION: The synthesis of membrane-bound non-specific acid phosphatase, strictly regulated by phosphate, and its properties suggest that this bacterium has a potential biotechnological application to solubilize phosphate in soils with low levels of this element, for specific crops. BioMed Central 2014-04-09 /pmc/articles/PMC3983855/ /pubmed/24713147 http://dx.doi.org/10.1186/1756-0500-7-221 Text en Copyright © 2014 Rombola et al.; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Research Article Rombola, Tiago Henrique Pedrinho, Eliamar Aparecida Nascimbem de Macedo Lemos, Eliana Gertrudes Gonçalves, Adriano Marques dos Santos, Luiz Flávio José Pizauro, João Martins Identification and enzymatic characterization of acid phosphatase from Burkholderia gladioli |
title | Identification and enzymatic characterization of acid phosphatase from Burkholderia gladioli |
title_full | Identification and enzymatic characterization of acid phosphatase from Burkholderia gladioli |
title_fullStr | Identification and enzymatic characterization of acid phosphatase from Burkholderia gladioli |
title_full_unstemmed | Identification and enzymatic characterization of acid phosphatase from Burkholderia gladioli |
title_short | Identification and enzymatic characterization of acid phosphatase from Burkholderia gladioli |
title_sort | identification and enzymatic characterization of acid phosphatase from burkholderia gladioli |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3983855/ https://www.ncbi.nlm.nih.gov/pubmed/24713147 http://dx.doi.org/10.1186/1756-0500-7-221 |
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