Halotolerant aminopeptidase M29 from Mesorhizobium SEMIA 3007 with biotechnological potential and its impact on biofilm synthesis
Autor(a) principal: | |
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Data de Publicação: | 2017 |
Outros Autores: | , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1038/s41598-017-10932-8 http://hdl.handle.net/11449/163210 |
Resumo: | The aminopeptidase gene from Mesorhizobium SEMIA3007 was cloned and overexpressed in Escherichia coli. The enzyme called MesoAmp exhibited optimum activity at pH 8.5 and 45 degrees C and was strongly activated by Co2+ and Mn2+. Under these reaction conditions, the enzyme displayed K-m and k(cat) values of 0.2364 +/- 0.018 mM and 712.1 +/- 88.12 s(-1), respectively. Additionally, the enzyme showed remarkable stability in organic solvents and was active at high concentrations of NaCl, suggesting that the enzyme might be suitable for use in biotechnology. MesoAmp is responsible for 40% of the organism's aminopeptidase activity. However, the enzyme's absence does not affect bacterial growth in synthetic broth, although it interfered with biofilm synthesis and osmoregulation. To the best of our knowledge, this report describes the first detailed characterization of aminopeptidase from Mesorhizobium and suggests its importance in biofilm formation and osmotic stress tolerance. In summary, this work lays the foundation for potential biotechnological applications and/or the development of environmentally friendly technologies and describes the first solvent- and halo-tolerant aminopeptidases identified from the Mesorhizobium genus and its importance in bacterial metabolism. |
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Halotolerant aminopeptidase M29 from Mesorhizobium SEMIA 3007 with biotechnological potential and its impact on biofilm synthesisThe aminopeptidase gene from Mesorhizobium SEMIA3007 was cloned and overexpressed in Escherichia coli. The enzyme called MesoAmp exhibited optimum activity at pH 8.5 and 45 degrees C and was strongly activated by Co2+ and Mn2+. Under these reaction conditions, the enzyme displayed K-m and k(cat) values of 0.2364 +/- 0.018 mM and 712.1 +/- 88.12 s(-1), respectively. Additionally, the enzyme showed remarkable stability in organic solvents and was active at high concentrations of NaCl, suggesting that the enzyme might be suitable for use in biotechnology. MesoAmp is responsible for 40% of the organism's aminopeptidase activity. However, the enzyme's absence does not affect bacterial growth in synthetic broth, although it interfered with biofilm synthesis and osmoregulation. To the best of our knowledge, this report describes the first detailed characterization of aminopeptidase from Mesorhizobium and suggests its importance in biofilm formation and osmotic stress tolerance. In summary, this work lays the foundation for potential biotechnological applications and/or the development of environmentally friendly technologies and describes the first solvent- and halo-tolerant aminopeptidases identified from the Mesorhizobium genus and its importance in bacterial metabolism.Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Sao Paulo State Univ, Dept Technol, Jaboticabal, SP, BrazilInst Res Bioenergy IPBEN, Jaboticabal, SP, BrazilUniv Simon Bolivar, Barranquilla, ColombiaAv Prof Paulo Donato Castellane S-N, BR-14884900 Jaboticabal, SP, BrazilSao Paulo State Univ, Dept Technol, Jaboticabal, SP, BrazilNature Publishing GroupUniversidade Estadual Paulista (Unesp)Inst Res Bioenergy IPBENUniv Simon BolivarSierra, Elwi Machado [UNESP]Pereira, Mariana RangelMaester, Thais CarvalhoGomes-Pepe, Elisangela Soares [UNESP]Mendoza, Elkin Rodas [UNESP]Macedo Lemos, Eliana G. de [UNESP]2018-11-26T17:40:31Z2018-11-26T17:40:31Z2017-09-06info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article14application/pdfhttp://dx.doi.org/10.1038/s41598-017-10932-8Scientific Reports. London: Nature Publishing Group, v. 7, 14 p., 2017.2045-2322http://hdl.handle.net/11449/16321010.1038/s41598-017-10932-8WOS:000409439900102WOS000409439900102.pdfWeb of Sciencereponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengScientific Reports1,533info:eu-repo/semantics/openAccess2024-06-07T15:32:34Zoai:repositorio.unesp.br:11449/163210Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T21:44:44.062426Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Halotolerant aminopeptidase M29 from Mesorhizobium SEMIA 3007 with biotechnological potential and its impact on biofilm synthesis |
title |
Halotolerant aminopeptidase M29 from Mesorhizobium SEMIA 3007 with biotechnological potential and its impact on biofilm synthesis |
spellingShingle |
Halotolerant aminopeptidase M29 from Mesorhizobium SEMIA 3007 with biotechnological potential and its impact on biofilm synthesis Sierra, Elwi Machado [UNESP] |
title_short |
Halotolerant aminopeptidase M29 from Mesorhizobium SEMIA 3007 with biotechnological potential and its impact on biofilm synthesis |
title_full |
Halotolerant aminopeptidase M29 from Mesorhizobium SEMIA 3007 with biotechnological potential and its impact on biofilm synthesis |
title_fullStr |
Halotolerant aminopeptidase M29 from Mesorhizobium SEMIA 3007 with biotechnological potential and its impact on biofilm synthesis |
title_full_unstemmed |
Halotolerant aminopeptidase M29 from Mesorhizobium SEMIA 3007 with biotechnological potential and its impact on biofilm synthesis |
title_sort |
Halotolerant aminopeptidase M29 from Mesorhizobium SEMIA 3007 with biotechnological potential and its impact on biofilm synthesis |
author |
Sierra, Elwi Machado [UNESP] |
author_facet |
Sierra, Elwi Machado [UNESP] Pereira, Mariana Rangel Maester, Thais Carvalho Gomes-Pepe, Elisangela Soares [UNESP] Mendoza, Elkin Rodas [UNESP] Macedo Lemos, Eliana G. de [UNESP] |
author_role |
author |
author2 |
Pereira, Mariana Rangel Maester, Thais Carvalho Gomes-Pepe, Elisangela Soares [UNESP] Mendoza, Elkin Rodas [UNESP] Macedo Lemos, Eliana G. de [UNESP] |
author2_role |
author author author author author |
dc.contributor.none.fl_str_mv |
Universidade Estadual Paulista (Unesp) Inst Res Bioenergy IPBEN Univ Simon Bolivar |
dc.contributor.author.fl_str_mv |
Sierra, Elwi Machado [UNESP] Pereira, Mariana Rangel Maester, Thais Carvalho Gomes-Pepe, Elisangela Soares [UNESP] Mendoza, Elkin Rodas [UNESP] Macedo Lemos, Eliana G. de [UNESP] |
description |
The aminopeptidase gene from Mesorhizobium SEMIA3007 was cloned and overexpressed in Escherichia coli. The enzyme called MesoAmp exhibited optimum activity at pH 8.5 and 45 degrees C and was strongly activated by Co2+ and Mn2+. Under these reaction conditions, the enzyme displayed K-m and k(cat) values of 0.2364 +/- 0.018 mM and 712.1 +/- 88.12 s(-1), respectively. Additionally, the enzyme showed remarkable stability in organic solvents and was active at high concentrations of NaCl, suggesting that the enzyme might be suitable for use in biotechnology. MesoAmp is responsible for 40% of the organism's aminopeptidase activity. However, the enzyme's absence does not affect bacterial growth in synthetic broth, although it interfered with biofilm synthesis and osmoregulation. To the best of our knowledge, this report describes the first detailed characterization of aminopeptidase from Mesorhizobium and suggests its importance in biofilm formation and osmotic stress tolerance. In summary, this work lays the foundation for potential biotechnological applications and/or the development of environmentally friendly technologies and describes the first solvent- and halo-tolerant aminopeptidases identified from the Mesorhizobium genus and its importance in bacterial metabolism. |
publishDate |
2017 |
dc.date.none.fl_str_mv |
2017-09-06 2018-11-26T17:40:31Z 2018-11-26T17:40:31Z |
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://dx.doi.org/10.1038/s41598-017-10932-8 Scientific Reports. London: Nature Publishing Group, v. 7, 14 p., 2017. 2045-2322 http://hdl.handle.net/11449/163210 10.1038/s41598-017-10932-8 WOS:000409439900102 WOS000409439900102.pdf |
url |
http://dx.doi.org/10.1038/s41598-017-10932-8 http://hdl.handle.net/11449/163210 |
identifier_str_mv |
Scientific Reports. London: Nature Publishing Group, v. 7, 14 p., 2017. 2045-2322 10.1038/s41598-017-10932-8 WOS:000409439900102 WOS000409439900102.pdf |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Scientific Reports 1,533 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
14 application/pdf |
dc.publisher.none.fl_str_mv |
Nature Publishing Group |
publisher.none.fl_str_mv |
Nature Publishing Group |
dc.source.none.fl_str_mv |
Web of Science 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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1808129353652895744 |