Halotolerant aminopeptidase M29 from Mesorhizobium SEMIA 3007 with biotechnological potential and its impact on biofilm synthesis

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 °C and was strongly activated by Co2+ and Mn2+. Under these reaction conditions, the enzyme displayed Km and kcat values of 0.2...

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Autores:
Machado Sierra, Elwi
Rangel Pereira, Mariana
Carvalho Maester, Thaís
Soares Gomes-Pepe, Elisangela
Rodas Mendoza, Elkin
Macedo Lemos, Elkin
Tipo de recurso:
Fecha de publicación:
2017
Institución:
Universidad Simón Bolívar
Repositorio:
Repositorio Digital USB
Idioma:
eng
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oai:bonga.unisimon.edu.co:20.500.12442/1585
Acceso en línea:
http://hdl.handle.net/20.500.12442/1585
Palabra clave:
Mesorhizobium
Aminopeptidase
Microbial Biofilms
Sodium Chloride
Osmosis
Biotechnology
Water-Electrolyte Balance
Organic solvent product
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License
licencia de Creative Commons Reconocimiento-NoComercial-CompartirIgual 4.0 Internacional
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oai_identifier_str oai:bonga.unisimon.edu.co:20.500.12442/1585
network_acronym_str USIMONBOL2
network_name_str Repositorio Digital USB
repository_id_str
dc.title.eng.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
Mesorhizobium
Aminopeptidase
Microbial Biofilms
Sodium Chloride
Osmosis
Biotechnology
Water-Electrolyte Balance
Organic solvent product
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
dc.creator.fl_str_mv Machado Sierra, Elwi
Rangel Pereira, Mariana
Carvalho Maester, Thaís
Soares Gomes-Pepe, Elisangela
Rodas Mendoza, Elkin
Macedo Lemos, Elkin
dc.contributor.author.none.fl_str_mv Machado Sierra, Elwi
Rangel Pereira, Mariana
Carvalho Maester, Thaís
Soares Gomes-Pepe, Elisangela
Rodas Mendoza, Elkin
Macedo Lemos, Elkin
dc.subject.eng.fl_str_mv Mesorhizobium
Aminopeptidase
Microbial Biofilms
Sodium Chloride
Osmosis
Biotechnology
Water-Electrolyte Balance
Organic solvent product
topic Mesorhizobium
Aminopeptidase
Microbial Biofilms
Sodium Chloride
Osmosis
Biotechnology
Water-Electrolyte Balance
Organic solvent product
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 °C and was strongly activated by Co2+ and Mn2+. Under these reaction conditions, the enzyme displayed Km and kcat 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.issued.none.fl_str_mv 2017-09-06
dc.date.accessioned.none.fl_str_mv 2018-02-05T14:41:30Z
dc.date.available.none.fl_str_mv 2018-02-05T14:41:30Z
dc.type.spa.fl_str_mv article
dc.type.coar.fl_str_mv http://purl.org/coar/resource_type/c_6501
dc.identifier.issn.none.fl_str_mv 20452322
dc.identifier.uri.none.fl_str_mv http://hdl.handle.net/20.500.12442/1585
identifier_str_mv 20452322
url http://hdl.handle.net/20.500.12442/1585
dc.language.iso.spa.fl_str_mv eng
language eng
dc.rights.coar.fl_str_mv http://purl.org/coar/access_right/c_abf2
dc.rights.license.spa.fl_str_mv licencia de Creative Commons Reconocimiento-NoComercial-CompartirIgual 4.0 Internacional
rights_invalid_str_mv licencia de Creative Commons Reconocimiento-NoComercial-CompartirIgual 4.0 Internacional
http://purl.org/coar/access_right/c_abf2
dc.publisher.spa.fl_str_mv Springer
dc.source.eng.fl_str_mv Scientific Reports
dc.source.none.fl_str_mv Vol. 7, No. 10684 (2017)
institution Universidad Simón Bolívar
dc.source.uri.eng.fl_str_mv DOI:10.1038/s41598-017-10932-8
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spelling licencia de Creative Commons Reconocimiento-NoComercial-CompartirIgual 4.0 Internacionalhttp://purl.org/coar/access_right/c_abf2Machado Sierra, Elwic4e7bb2a-d0dc-4b8b-8222-f6b6daf5b678Rangel Pereira, Marianab52edd75-ac95-45c0-b964-eeafdca55593Carvalho Maester, Thaís78cfda06-ac7e-46e8-a299-8668a67e542fSoares Gomes-Pepe, Elisangela90d1b92d-918c-4379-9f7b-4c24850a2c6eRodas Mendoza, Elkin9b1dd5a9-d1be-424a-b187-f0bf695bf26bMacedo Lemos, Elkin06af8b10-9b0b-450a-a833-d6e6018753192018-02-05T14:41:30Z2018-02-05T14:41:30Z2017-09-0620452322http://hdl.handle.net/20.500.12442/1585The 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 °C and was strongly activated by Co2+ and Mn2+. Under these reaction conditions, the enzyme displayed Km and kcat 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.engSpringerScientific ReportsVol. 7, No. 10684 (2017)DOI:10.1038/s41598-017-10932-8MesorhizobiumAminopeptidaseMicrobial BiofilmsSodium ChlorideOsmosisBiotechnologyWater-Electrolyte BalanceOrganic solvent productHalotolerant aminopeptidase M29 from Mesorhizobium SEMIA 3007 with biotechnological potential and its impact on biofilm synthesisarticlehttp://purl.org/coar/resource_type/c_6501Ghobakhlou, A.-F., Johnston, A., Harris, L., Antoun, H. & Laberge, S. Microarray transcriptional profiling of Arctic Mesorhizobium strain N33 at low temperature provides insights into cold adaption strategies. BMC Genomics 16, 383 (2015).Krick, A. et al. A Marine Mesorhizobium sp. 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Cloning and characterization of a novel β-transaminase from Mesorhizobium sp. strain LUK: A new biocatalyst for the synthesis of enantiomerically pure??-amino acids. Appl. Environ. Microbiol. 73, 1772–1782 (2007).Prasad, M. P. & Sethi, R. Optimization of cellulase production from a novel bacterial isolate Mesorhizobium sp. from marine source. J. Enzym. Res. 4, 39–45 (2013).Takata, G. et al. Characterization of Mesorhizobium loti L -Rhamnose Isomerase and Its Application to L -Talose Production. Biosci. Biotechnol. Biochem. 75, 1006–1009 (2011).Mugo, A. N. et al. Crystal structure of pyridoxine 4-oxidase from Mesorhizobium loti. Biochim. Biophys. Acta 1834, 953–63 (2013).Huang, W. et al. The Structure and Enzyme Characteristics of a Recombinant Leucine Aminopeptidase rLap1 from Aspergillus sojae and Its Application in Debittering. Appl. Biochem. Biotechnol. 177, 190–206 (2015).Thomas, S., Besset, C., Courtin, P. & Rul, F. 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Microbiol. 85, 561–566 (1998).ORIGINALPDF.pdfPDF.pdfFormato Pdf texto completoapplication/pdf1765996https://bonga.unisimon.edu.co/bitstreams/035fcd91-23ae-48a1-b57e-ff7057d1501f/downloadb2ca57fbd56ea27d399a02bd0a56ada9MD51LICENSElicense.txtlicense.txttext/plain; charset=utf-81748https://bonga.unisimon.edu.co/bitstreams/9d01a6d3-e6d7-483b-8317-1d4fd0cf0156/download8a4605be74aa9ea9d79846c1fba20a33MD52TEXT2017_Halotolerant (1).pdf.txt2017_Halotolerant (1).pdf.txtExtracted texttext/plain67277https://bonga.unisimon.edu.co/bitstreams/b3fa0171-4214-4425-a104-b688bc711a7d/download83777acb9290acb602713215c23f9fe8MD53PDF.pdf.txtPDF.pdf.txtExtracted texttext/plain70299https://bonga.unisimon.edu.co/bitstreams/33d7b425-ff47-4198-9da6-d333f6545bdc/download37b65189f6ace8fec270cd0f68300266MD55THUMBNAIL2017_Halotolerant (1).pdf.jpg2017_Halotolerant (1).pdf.jpgGenerated Thumbnailimage/jpeg1921https://bonga.unisimon.edu.co/bitstreams/71f7a1e8-75ad-4b59-acaf-d6387e1cb68a/download208507ad17fd92410c691812efecda40MD54PDF.pdf.jpgPDF.pdf.jpgGenerated Thumbnailimage/jpeg6672https://bonga.unisimon.edu.co/bitstreams/da005348-a515-4a85-ad51-0bc88eab603b/download7a1e9ddcd2afa0e142e2b899e6d1e56dMD5620.500.12442/1585oai:bonga.unisimon.edu.co:20.500.12442/15852024-08-14 21:52:58.801open.accesshttps://bonga.unisimon.edu.coRepositorio Digital Universidad Simón Bolívarrepositorio.digital@unisimon.edu.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