Enzymatic reduction and oxidation of fibre-bound azo-dyes

Detalhes bibliográficos
Autor(a) principal: Pricelius, S.
Data de Publicação: 2007
Outros Autores: Held, C., Sollner, S., Deller, S., Murkovic, M., Ullrich, R., Hofrichter, M., Paulo, Artur Cavaco, Macheroux, P., Guebitz, G. M.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/1822/13559
Resumo: A new customer and environmental friendly method of hair bound dye decolouration was developed. Biotransformation of the azo-dyes Flame Orange and Ruby Red was studied using different oxidoreductases. The pathways of azo dye conversion by these enzymes were investigated and the intermediates and metabolites were identified and characterised using UV–vis spectroscopy, high-performance liquid chromatography (HPLC) and mass spectrometry (MS). Laccase from Pycnoporus cinnabarinus, manganese peroxidase (MnP) from Nematoloma frowardii and the novel Agrocybe aegerita peroxidase (AaP) were found to use a similar mechanism to convert azo dyes. They N-demethylated the dyes and concomitantly polymerized them to some extent. On the other hand the mechanism for cleavage of the azo bond by azo-reductases of Bacillus cereus and B. subtilis was based on reduction of the azo bond at the expense of NAD(P)H.
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spelling Enzymatic reduction and oxidation of fibre-bound azo-dyesAzo dyeHairAzoreductaseLaccaseScience & TechnologyA new customer and environmental friendly method of hair bound dye decolouration was developed. Biotransformation of the azo-dyes Flame Orange and Ruby Red was studied using different oxidoreductases. The pathways of azo dye conversion by these enzymes were investigated and the intermediates and metabolites were identified and characterised using UV–vis spectroscopy, high-performance liquid chromatography (HPLC) and mass spectrometry (MS). Laccase from Pycnoporus cinnabarinus, manganese peroxidase (MnP) from Nematoloma frowardii and the novel Agrocybe aegerita peroxidase (AaP) were found to use a similar mechanism to convert azo dyes. They N-demethylated the dyes and concomitantly polymerized them to some extent. On the other hand the mechanism for cleavage of the azo bond by azo-reductases of Bacillus cereus and B. subtilis was based on reduction of the azo bond at the expense of NAD(P)H.ElsevierUniversidade do MinhoPricelius, S.Held, C.Sollner, S.Deller, S.Murkovic, M.Ullrich, R.Hofrichter, M.Paulo, Artur CavacoMacheroux, P.Guebitz, G. M.2007-062007-06-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/13559eng0141-022910.1016/j.enzmictec.2006.11.004http://www.sciencedirect.com/science/article/pii/S014102290600545Xinfo:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-07-21T12:11:28Zoai:repositorium.sdum.uminho.pt:1822/13559Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T19:03:15.428134Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Enzymatic reduction and oxidation of fibre-bound azo-dyes
title Enzymatic reduction and oxidation of fibre-bound azo-dyes
spellingShingle Enzymatic reduction and oxidation of fibre-bound azo-dyes
Pricelius, S.
Azo dye
Hair
Azoreductase
Laccase
Science & Technology
title_short Enzymatic reduction and oxidation of fibre-bound azo-dyes
title_full Enzymatic reduction and oxidation of fibre-bound azo-dyes
title_fullStr Enzymatic reduction and oxidation of fibre-bound azo-dyes
title_full_unstemmed Enzymatic reduction and oxidation of fibre-bound azo-dyes
title_sort Enzymatic reduction and oxidation of fibre-bound azo-dyes
author Pricelius, S.
author_facet Pricelius, S.
Held, C.
Sollner, S.
Deller, S.
Murkovic, M.
Ullrich, R.
Hofrichter, M.
Paulo, Artur Cavaco
Macheroux, P.
Guebitz, G. M.
author_role author
author2 Held, C.
Sollner, S.
Deller, S.
Murkovic, M.
Ullrich, R.
Hofrichter, M.
Paulo, Artur Cavaco
Macheroux, P.
Guebitz, G. M.
author2_role author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade do Minho
dc.contributor.author.fl_str_mv Pricelius, S.
Held, C.
Sollner, S.
Deller, S.
Murkovic, M.
Ullrich, R.
Hofrichter, M.
Paulo, Artur Cavaco
Macheroux, P.
Guebitz, G. M.
dc.subject.por.fl_str_mv Azo dye
Hair
Azoreductase
Laccase
Science & Technology
topic Azo dye
Hair
Azoreductase
Laccase
Science & Technology
description A new customer and environmental friendly method of hair bound dye decolouration was developed. Biotransformation of the azo-dyes Flame Orange and Ruby Red was studied using different oxidoreductases. The pathways of azo dye conversion by these enzymes were investigated and the intermediates and metabolites were identified and characterised using UV–vis spectroscopy, high-performance liquid chromatography (HPLC) and mass spectrometry (MS). Laccase from Pycnoporus cinnabarinus, manganese peroxidase (MnP) from Nematoloma frowardii and the novel Agrocybe aegerita peroxidase (AaP) were found to use a similar mechanism to convert azo dyes. They N-demethylated the dyes and concomitantly polymerized them to some extent. On the other hand the mechanism for cleavage of the azo bond by azo-reductases of Bacillus cereus and B. subtilis was based on reduction of the azo bond at the expense of NAD(P)H.
publishDate 2007
dc.date.none.fl_str_mv 2007-06
2007-06-01T00:00:00Z
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://hdl.handle.net/1822/13559
url http://hdl.handle.net/1822/13559
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 0141-0229
10.1016/j.enzmictec.2006.11.004
http://www.sciencedirect.com/science/article/pii/S014102290600545X
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
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reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
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