Properties of catechol 1,2-dioxygenase in the cell free extract and immobilized extract of Mycobacterium fortuitum
Autor(a) principal: | |
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Data de Publicação: | 2013 |
Outros Autores: | , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UFRGS |
Texto Completo: | http://hdl.handle.net/10183/107359 |
Resumo: | Polycyclic aromatic hydrocarbons (PAH) are carcinogenic compounds which contaminate water and soil, and the enzymes can be used for bioremediation of these environments. This study aimed to evaluate some environmental conditions that affect the production and activity of the catechol 1,2-dioxygenase (C12O) by Mycobacterium fortuitum in the cell free and immobilized extract in sodium alginate. The bacterium was grown in mineral medium and LB broth containing 250 mg L-1 of anthracene (PAH). The optimum conditions of pH (4.0-9.0), temperature (5-70 °C), reaction time (10-90 min) and the effect of ions in the enzyme activity were determined. The Mycobacterium cultivated in LB shown higher growth and the C12O activity was two-fold higher to that in the mineral medium. To both extracts the highest enzyme activity was at pH 8.0, however, the immobilized extract promoted the increase in the C12O activity in a pH range between 4.0 and 8.5. The immobilized extract increased the enzymatic activity time and showed the highest C12O activity at 45 °C, 20 °C higher than the greatest temperature in the cell free extract. The enzyme activity in both extracts was stimulated by Fe3+, Hg2+ and Mn2+ and inhibited by NH4+ and Cu2+, but the immobilization protected the enzyme against the deleterious effects of K+ and Mg2+ in tested concentrations. The catechol 1,2-dioxygenase of Mycobacterium fortuitum in the immobilized extract has greater stability to the variations of pH, temperature and reaction time, and show higher activity in presence of ions, comparing to the cell free extract. |
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Silva, Andréa Scaramal daJacques, Rodrigo Josemar SeminotiAndreazza, RobsonBento, Fatima MenezesRoesch, Luiz Fernando WurdigCamargo, Flavio Anastacio de Oliveira2014-11-22T02:17:11Z20131517-8382http://hdl.handle.net/10183/107359000941365Polycyclic aromatic hydrocarbons (PAH) are carcinogenic compounds which contaminate water and soil, and the enzymes can be used for bioremediation of these environments. This study aimed to evaluate some environmental conditions that affect the production and activity of the catechol 1,2-dioxygenase (C12O) by Mycobacterium fortuitum in the cell free and immobilized extract in sodium alginate. The bacterium was grown in mineral medium and LB broth containing 250 mg L-1 of anthracene (PAH). The optimum conditions of pH (4.0-9.0), temperature (5-70 °C), reaction time (10-90 min) and the effect of ions in the enzyme activity were determined. The Mycobacterium cultivated in LB shown higher growth and the C12O activity was two-fold higher to that in the mineral medium. To both extracts the highest enzyme activity was at pH 8.0, however, the immobilized extract promoted the increase in the C12O activity in a pH range between 4.0 and 8.5. The immobilized extract increased the enzymatic activity time and showed the highest C12O activity at 45 °C, 20 °C higher than the greatest temperature in the cell free extract. The enzyme activity in both extracts was stimulated by Fe3+, Hg2+ and Mn2+ and inhibited by NH4+ and Cu2+, but the immobilization protected the enzyme against the deleterious effects of K+ and Mg2+ in tested concentrations. The catechol 1,2-dioxygenase of Mycobacterium fortuitum in the immobilized extract has greater stability to the variations of pH, temperature and reaction time, and show higher activity in presence of ions, comparing to the cell free extract.application/pdfengBrazilian Journal of Microbiology. São Paulo, SP. Vol. 44, n. 1, (2013), p. 291-297EnzimaBiorremediaçãoBiodegradaçãoAnthraceneEnzyme activityEnzyme immobilizationBiodegradationWaste treatmentProperties of catechol 1,2-dioxygenase in the cell free extract and immobilized extract of Mycobacterium fortuituminfo:eu-repo/semantics/articleinfo:eu-repo/semantics/otherinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UFRGSinstname:Universidade Federal do Rio Grande do Sul (UFRGS)instacron:UFRGSORIGINAL000941365.pdf000941365.pdfTexto completo (inglês)application/pdf688768http://www.lume.ufrgs.br/bitstream/10183/107359/1/000941365.pdf9e9e6252670ab250f52dd0d4d0e065c0MD51TEXT000941365.pdf.txt000941365.pdf.txtExtracted Texttext/plain31717http://www.lume.ufrgs.br/bitstream/10183/107359/2/000941365.pdf.txt95b30efb6c2922b635c7990309414345MD52THUMBNAIL000941365.pdf.jpg000941365.pdf.jpgGenerated Thumbnailimage/jpeg1608http://www.lume.ufrgs.br/bitstream/10183/107359/3/000941365.pdf.jpg56181e89d6bb3ea380ca9f6c8189b00eMD5310183/1073592018-10-22 08:08:17.708oai:www.lume.ufrgs.br:10183/107359Repositório de PublicaçõesPUBhttps://lume.ufrgs.br/oai/requestopendoar:2018-10-22T11:08:17Repositório Institucional da UFRGS - Universidade Federal do Rio Grande do Sul (UFRGS)false |
dc.title.pt_BR.fl_str_mv |
Properties of catechol 1,2-dioxygenase in the cell free extract and immobilized extract of Mycobacterium fortuitum |
title |
Properties of catechol 1,2-dioxygenase in the cell free extract and immobilized extract of Mycobacterium fortuitum |
spellingShingle |
Properties of catechol 1,2-dioxygenase in the cell free extract and immobilized extract of Mycobacterium fortuitum Silva, Andréa Scaramal da Enzima Biorremediação Biodegradação Anthracene Enzyme activity Enzyme immobilization Biodegradation Waste treatment |
title_short |
Properties of catechol 1,2-dioxygenase in the cell free extract and immobilized extract of Mycobacterium fortuitum |
title_full |
Properties of catechol 1,2-dioxygenase in the cell free extract and immobilized extract of Mycobacterium fortuitum |
title_fullStr |
Properties of catechol 1,2-dioxygenase in the cell free extract and immobilized extract of Mycobacterium fortuitum |
title_full_unstemmed |
Properties of catechol 1,2-dioxygenase in the cell free extract and immobilized extract of Mycobacterium fortuitum |
title_sort |
Properties of catechol 1,2-dioxygenase in the cell free extract and immobilized extract of Mycobacterium fortuitum |
author |
Silva, Andréa Scaramal da |
author_facet |
Silva, Andréa Scaramal da Jacques, Rodrigo Josemar Seminoti Andreazza, Robson Bento, Fatima Menezes Roesch, Luiz Fernando Wurdig Camargo, Flavio Anastacio de Oliveira |
author_role |
author |
author2 |
Jacques, Rodrigo Josemar Seminoti Andreazza, Robson Bento, Fatima Menezes Roesch, Luiz Fernando Wurdig Camargo, Flavio Anastacio de Oliveira |
author2_role |
author author author author author |
dc.contributor.author.fl_str_mv |
Silva, Andréa Scaramal da Jacques, Rodrigo Josemar Seminoti Andreazza, Robson Bento, Fatima Menezes Roesch, Luiz Fernando Wurdig Camargo, Flavio Anastacio de Oliveira |
dc.subject.por.fl_str_mv |
Enzima Biorremediação Biodegradação |
topic |
Enzima Biorremediação Biodegradação Anthracene Enzyme activity Enzyme immobilization Biodegradation Waste treatment |
dc.subject.eng.fl_str_mv |
Anthracene Enzyme activity Enzyme immobilization Biodegradation Waste treatment |
description |
Polycyclic aromatic hydrocarbons (PAH) are carcinogenic compounds which contaminate water and soil, and the enzymes can be used for bioremediation of these environments. This study aimed to evaluate some environmental conditions that affect the production and activity of the catechol 1,2-dioxygenase (C12O) by Mycobacterium fortuitum in the cell free and immobilized extract in sodium alginate. The bacterium was grown in mineral medium and LB broth containing 250 mg L-1 of anthracene (PAH). The optimum conditions of pH (4.0-9.0), temperature (5-70 °C), reaction time (10-90 min) and the effect of ions in the enzyme activity were determined. The Mycobacterium cultivated in LB shown higher growth and the C12O activity was two-fold higher to that in the mineral medium. To both extracts the highest enzyme activity was at pH 8.0, however, the immobilized extract promoted the increase in the C12O activity in a pH range between 4.0 and 8.5. The immobilized extract increased the enzymatic activity time and showed the highest C12O activity at 45 °C, 20 °C higher than the greatest temperature in the cell free extract. The enzyme activity in both extracts was stimulated by Fe3+, Hg2+ and Mn2+ and inhibited by NH4+ and Cu2+, but the immobilization protected the enzyme against the deleterious effects of K+ and Mg2+ in tested concentrations. The catechol 1,2-dioxygenase of Mycobacterium fortuitum in the immobilized extract has greater stability to the variations of pH, temperature and reaction time, and show higher activity in presence of ions, comparing to the cell free extract. |
publishDate |
2013 |
dc.date.issued.fl_str_mv |
2013 |
dc.date.accessioned.fl_str_mv |
2014-11-22T02:17:11Z |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/other |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10183/107359 |
dc.identifier.issn.pt_BR.fl_str_mv |
1517-8382 |
dc.identifier.nrb.pt_BR.fl_str_mv |
000941365 |
identifier_str_mv |
1517-8382 000941365 |
url |
http://hdl.handle.net/10183/107359 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.ispartof.pt_BR.fl_str_mv |
Brazilian Journal of Microbiology. São Paulo, SP. Vol. 44, n. 1, (2013), p. 291-297 |
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info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
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application/pdf |
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