Enzymatic activity of catechol 1,2-dioxygenase and catechol 2,3-dioxygenase produced by Gordonia polyisoprenivorans

Detalhes bibliográficos
Autor(a) principal: Silva, Andréa Scaramal da
Data de Publicação: 2012
Outros Autores: Camargo, Flavio Anastacio de Oliveira, Andreazza, Robson, Jacques, Rodrigo Josemar Seminoti, Baldoni, Daiane Bortoluzzi, Bento, Fatima Menezes
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UFRGS
Texto Completo: http://hdl.handle.net/10183/107357
Resumo: This study aimed to evaluate the environmental conditions for enzyme activity of catechol 1,2-dioxygenase (C1,2O) and catechol 2,3-dioxygenase (C2,3O) produced by Gordonia polyisoprenivorans in cell-free and immobilized extracts. The optimum conditions of pH, temperature, time course and effect of ions for enzyme activity were determined. Peak activity of C1,2O occurred at pH 8.0. The isolate exhibited the highest activity of C2,3O at pH 7.0 and 8.0 for the cell-free extract and immobilized extract, respectively. This isolate exhibited important characteristics such as broad range of pH, temperature and time course for enzyme activity.
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spelling Silva, Andréa Scaramal daCamargo, Flavio Anastacio de OliveiraAndreazza, RobsonJacques, Rodrigo Josemar SeminotiBaldoni, Daiane BortoluzziBento, Fatima Menezes2014-11-22T02:17:11Z20120100-4042http://hdl.handle.net/10183/107357000941256This study aimed to evaluate the environmental conditions for enzyme activity of catechol 1,2-dioxygenase (C1,2O) and catechol 2,3-dioxygenase (C2,3O) produced by Gordonia polyisoprenivorans in cell-free and immobilized extracts. The optimum conditions of pH, temperature, time course and effect of ions for enzyme activity were determined. Peak activity of C1,2O occurred at pH 8.0. The isolate exhibited the highest activity of C2,3O at pH 7.0 and 8.0 for the cell-free extract and immobilized extract, respectively. This isolate exhibited important characteristics such as broad range of pH, temperature and time course for enzyme activity.application/pdfengQuímica nova. São Paulo. Vol. 35, n.8 (2012), p. 1587-1592BiodegradaçãoBiorremediaçãoTratamento de esgotoAnthraceneEnzyme activityEnzyme immobilizationEnzymatic activity of catechol 1,2-dioxygenase and catechol 2,3-dioxygenase produced by Gordonia polyisoprenivoransinfo: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:UFRGSORIGINAL000941256.pdf000941256.pdfTexto completo (inglês)application/pdf378112http://www.lume.ufrgs.br/bitstream/10183/107357/1/000941256.pdf9c8ed5bc8ae30f9c442a3ef08148a9efMD51TEXT000941256.pdf.txt000941256.pdf.txtExtracted Texttext/plain28325http://www.lume.ufrgs.br/bitstream/10183/107357/2/000941256.pdf.txtd1e8d13085c1b9d6607cfdc639ebcc8fMD52THUMBNAIL000941256.pdf.jpg000941256.pdf.jpgGenerated Thumbnailimage/jpeg1893http://www.lume.ufrgs.br/bitstream/10183/107357/3/000941256.pdf.jpg29fcb3b5cbe7091431b7ae53f2be216dMD5310183/1073572018-10-22 08:08:16.823oai:www.lume.ufrgs.br:10183/107357Repositório de PublicaçõesPUBhttps://lume.ufrgs.br/oai/requestopendoar:2018-10-22T11:08:16Repositório Institucional da UFRGS - Universidade Federal do Rio Grande do Sul (UFRGS)false
dc.title.pt_BR.fl_str_mv Enzymatic activity of catechol 1,2-dioxygenase and catechol 2,3-dioxygenase produced by Gordonia polyisoprenivorans
title Enzymatic activity of catechol 1,2-dioxygenase and catechol 2,3-dioxygenase produced by Gordonia polyisoprenivorans
spellingShingle Enzymatic activity of catechol 1,2-dioxygenase and catechol 2,3-dioxygenase produced by Gordonia polyisoprenivorans
Silva, Andréa Scaramal da
Biodegradação
Biorremediação
Tratamento de esgoto
Anthracene
Enzyme activity
Enzyme immobilization
title_short Enzymatic activity of catechol 1,2-dioxygenase and catechol 2,3-dioxygenase produced by Gordonia polyisoprenivorans
title_full Enzymatic activity of catechol 1,2-dioxygenase and catechol 2,3-dioxygenase produced by Gordonia polyisoprenivorans
title_fullStr Enzymatic activity of catechol 1,2-dioxygenase and catechol 2,3-dioxygenase produced by Gordonia polyisoprenivorans
title_full_unstemmed Enzymatic activity of catechol 1,2-dioxygenase and catechol 2,3-dioxygenase produced by Gordonia polyisoprenivorans
title_sort Enzymatic activity of catechol 1,2-dioxygenase and catechol 2,3-dioxygenase produced by Gordonia polyisoprenivorans
author Silva, Andréa Scaramal da
author_facet Silva, Andréa Scaramal da
Camargo, Flavio Anastacio de Oliveira
Andreazza, Robson
Jacques, Rodrigo Josemar Seminoti
Baldoni, Daiane Bortoluzzi
Bento, Fatima Menezes
author_role author
author2 Camargo, Flavio Anastacio de Oliveira
Andreazza, Robson
Jacques, Rodrigo Josemar Seminoti
Baldoni, Daiane Bortoluzzi
Bento, Fatima Menezes
author2_role author
author
author
author
author
dc.contributor.author.fl_str_mv Silva, Andréa Scaramal da
Camargo, Flavio Anastacio de Oliveira
Andreazza, Robson
Jacques, Rodrigo Josemar Seminoti
Baldoni, Daiane Bortoluzzi
Bento, Fatima Menezes
dc.subject.por.fl_str_mv Biodegradação
Biorremediação
Tratamento de esgoto
topic Biodegradação
Biorremediação
Tratamento de esgoto
Anthracene
Enzyme activity
Enzyme immobilization
dc.subject.eng.fl_str_mv Anthracene
Enzyme activity
Enzyme immobilization
description This study aimed to evaluate the environmental conditions for enzyme activity of catechol 1,2-dioxygenase (C1,2O) and catechol 2,3-dioxygenase (C2,3O) produced by Gordonia polyisoprenivorans in cell-free and immobilized extracts. The optimum conditions of pH, temperature, time course and effect of ions for enzyme activity were determined. Peak activity of C1,2O occurred at pH 8.0. The isolate exhibited the highest activity of C2,3O at pH 7.0 and 8.0 for the cell-free extract and immobilized extract, respectively. This isolate exhibited important characteristics such as broad range of pH, temperature and time course for enzyme activity.
publishDate 2012
dc.date.issued.fl_str_mv 2012
dc.date.accessioned.fl_str_mv 2014-11-22T02:17:11Z
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dc.identifier.uri.fl_str_mv http://hdl.handle.net/10183/107357
dc.identifier.issn.pt_BR.fl_str_mv 0100-4042
dc.identifier.nrb.pt_BR.fl_str_mv 000941256
identifier_str_mv 0100-4042
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url http://hdl.handle.net/10183/107357
dc.language.iso.fl_str_mv eng
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dc.relation.ispartof.pt_BR.fl_str_mv Química nova. São Paulo. Vol. 35, n.8 (2012), p. 1587-1592
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instname:Universidade Federal do Rio Grande do Sul (UFRGS)
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instname_str Universidade Federal do Rio Grande do Sul (UFRGS)
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reponame_str Repositório Institucional da UFRGS
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