Enzymatic activity of catechol 1,2-dioxygenase and catechol 2,3-dioxygenase produced by Gordonia polyisoprenivorans
dc.contributor.author | Silva, Andréa Scaramal da | pt_BR |
dc.contributor.author | Camargo, Flavio Anastacio de Oliveira | pt_BR |
dc.contributor.author | Andreazza, Robson | pt_BR |
dc.contributor.author | Jacques, Rodrigo Josemar Seminoti | pt_BR |
dc.contributor.author | Baldoni, Daiane Bortoluzzi | pt_BR |
dc.contributor.author | Bento, Fatima Menezes | pt_BR |
dc.date.accessioned | 2014-11-22T02:17:11Z | pt_BR |
dc.date.issued | 2012 | pt_BR |
dc.identifier.issn | 0100-4042 | pt_BR |
dc.identifier.uri | http://hdl.handle.net/10183/107357 | pt_BR |
dc.description.abstract | 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. | en |
dc.format.mimetype | application/pdf | |
dc.language.iso | eng | pt_BR |
dc.relation.ispartof | Química nova. São Paulo. Vol. 35, n.8 (2012), p. 1587-1592 | pt_BR |
dc.rights | Open Access | en |
dc.subject | Anthracene | en |
dc.subject | Biodegradação | pt_BR |
dc.subject | Enzyme activity | en |
dc.subject | Biorremediação | pt_BR |
dc.subject | Tratamento de esgoto | pt_BR |
dc.subject | Enzyme immobilization | en |
dc.title | Enzymatic activity of catechol 1,2-dioxygenase and catechol 2,3-dioxygenase produced by Gordonia polyisoprenivorans | pt_BR |
dc.type | Artigo de periódico | pt_BR |
dc.identifier.nrb | 000941256 | pt_BR |
dc.type.origin | Nacional | pt_BR |
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