Identification and enzymatic characterization of acid phosphatase from Burkholderia gladioli
Autor(a) principal: | |
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Data de Publicação: | 2014 |
Outros Autores: | , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://www.biomedcentral.com/1756-0500/7/221 http://hdl.handle.net/11449/123618 |
Resumo: | 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, Vm = 113.5 U/mg and K0.5 = 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. |
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Repositório Institucional da UNESP |
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2946 |
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Identification and enzymatic characterization of acid phosphatase from Burkholderia gladioliPhosphohydrolaseInhibitionPhosphateP-NitrophenylphosphateSolubilizationBackground: 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, Vm = 113.5 U/mg and K0.5 = 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.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Universidade Estadual Paulista Júlio de Mesquita Filho, Departamento de Tecnologia, Faculadade de Ciências Agrárias e Veterinárias Jaboticabal, Jaboticabal, Via deAcesso Prof Paulo Donato Castellani s/n, Rural, CEP 14884-900, SP, BrasilUniversidade Estadual Paulista Júlio de Mesquita Filho, Departamento de Tecnologia, Faculadade de Ciências Agrárias e Veterinárias Jaboticabal, Jaboticabal, Via deAcesso Prof Paulo Donato Castellani s/n, Rural, CEP 14884-900, SP, BrasilFaculdade de Ciências Agrárias e Veterinárias (FCAV), UNESP – Univ Estadual Paulista, Câmpus de Jaboticabal, Departamento de Tecnologia, Laboratório de Enzimologia Aplicada, Jaboticabal, SP, BrazilInstituto de Química (IQ), Univ Estadual Paulista, Câmpus de Araraquara, Araraquara, SP, BrazilUniversidade Estadual Paulista (Unesp)Rombola, Tiago Henrique [UNESP]Pedrinho, Eliamar Aparecida Nascimbem [UNESP]Lemos, Eliana Gertrudes Macedo [UNESP]Gonçalves, Adriano Marques [UNESP]Santos, Luiz Flávio José dos [UNESP]Pizauro Júnior, João Martins [UNESP]2015-05-15T13:30:30Z2015-05-15T13:30:30Z2014info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article221-227application/pdfhttp://www.biomedcentral.com/1756-0500/7/221BMC Research Notes, v. 7, p. 221-227, 2014.1756-0500http://hdl.handle.net/11449/12361810.1186/1756-0500-7-221ISSN1756-0500-2014-07-221-227.pdf3958124498479090390202093648094354482035956280745888302973425312Currículo Lattesreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengBMC Research Notes0,691info:eu-repo/semantics/openAccess2023-10-04T06:03:12Zoai:repositorio.unesp.br:11449/123618Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462023-10-04T06:03:12Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Identification and enzymatic characterization of acid phosphatase from Burkholderia gladioli |
title |
Identification and enzymatic characterization of acid phosphatase from Burkholderia gladioli |
spellingShingle |
Identification and enzymatic characterization of acid phosphatase from Burkholderia gladioli Rombola, Tiago Henrique [UNESP] Phosphohydrolase Inhibition Phosphate P-Nitrophenylphosphate Solubilization |
title_short |
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_sort |
Identification and enzymatic characterization of acid phosphatase from Burkholderia gladioli |
author |
Rombola, Tiago Henrique [UNESP] |
author_facet |
Rombola, Tiago Henrique [UNESP] Pedrinho, Eliamar Aparecida Nascimbem [UNESP] Lemos, Eliana Gertrudes Macedo [UNESP] Gonçalves, Adriano Marques [UNESP] Santos, Luiz Flávio José dos [UNESP] Pizauro Júnior, João Martins [UNESP] |
author_role |
author |
author2 |
Pedrinho, Eliamar Aparecida Nascimbem [UNESP] Lemos, Eliana Gertrudes Macedo [UNESP] Gonçalves, Adriano Marques [UNESP] Santos, Luiz Flávio José dos [UNESP] Pizauro Júnior, João Martins [UNESP] |
author2_role |
author author author author author |
dc.contributor.none.fl_str_mv |
Universidade Estadual Paulista (Unesp) |
dc.contributor.author.fl_str_mv |
Rombola, Tiago Henrique [UNESP] Pedrinho, Eliamar Aparecida Nascimbem [UNESP] Lemos, Eliana Gertrudes Macedo [UNESP] Gonçalves, Adriano Marques [UNESP] Santos, Luiz Flávio José dos [UNESP] Pizauro Júnior, João Martins [UNESP] |
dc.subject.por.fl_str_mv |
Phosphohydrolase Inhibition Phosphate P-Nitrophenylphosphate Solubilization |
topic |
Phosphohydrolase Inhibition Phosphate P-Nitrophenylphosphate Solubilization |
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, Vm = 113.5 U/mg and K0.5 = 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. |
publishDate |
2014 |
dc.date.none.fl_str_mv |
2014 2015-05-15T13:30:30Z 2015-05-15T13:30:30Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://www.biomedcentral.com/1756-0500/7/221 BMC Research Notes, v. 7, p. 221-227, 2014. 1756-0500 http://hdl.handle.net/11449/123618 10.1186/1756-0500-7-221 ISSN1756-0500-2014-07-221-227.pdf 3958124498479090 3902020936480943 5448203595628074 5888302973425312 |
url |
http://www.biomedcentral.com/1756-0500/7/221 http://hdl.handle.net/11449/123618 |
identifier_str_mv |
BMC Research Notes, v. 7, p. 221-227, 2014. 1756-0500 10.1186/1756-0500-7-221 ISSN1756-0500-2014-07-221-227.pdf 3958124498479090 3902020936480943 5448203595628074 5888302973425312 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
BMC Research Notes 0,691 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
221-227 application/pdf |
dc.source.none.fl_str_mv |
Currículo Lattes reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
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1799964427267604480 |