Specificities of a chemically modified laccase from trametes hirsuta on soluble and cellulose-bound substrates

Detalhes bibliográficos
Autor(a) principal: Schroeder, M.
Data de Publicação: 2006
Outros Autores: Heumann, Sonja, Silva, Carla J. S. M., Paulo, Artur Cavaco, Gübitz, Georg 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/1822/12948
Resumo: Laccases could prevent fabrics and garments from re-deposition of dyes during washing and finishing processes by degrading the solubilized dye. However, laccase action must be restricted to solubilized dye molecules thereby avoiding decolorization of fabrics. Chemical modification of enzymes can provide a powerful tool to change the adsorption behaviour of enzymes on water insoluble polymers. Polyethylene glycol (PEG) was covalently attached onto a laccase from Trametes hirsuta. Different molecular weights of the synthetic polymer were tested in terms of adsorption behaviour and retained laccase activity. Covalent attachment of PEG onto the laccase resulted in enhanced enzyme stability while with increasing molecular weight of attached PEG the substrate affinity for the laccase conjugate decreased. The activity of the modified laccases on fibre bound dye was drastically reduced decreasing the adsorption of the enzyme on various fabrics. Compared to the 5 kDa PEG laccase conjugate (K/S value 47.60)
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spelling Specificities of a chemically modified laccase from trametes hirsuta on soluble and cellulose-bound substratesLaccasePolyethylene glycolDye-degradingEnzyme modificationTrametes hirsutaScience & TechnologyLaccases could prevent fabrics and garments from re-deposition of dyes during washing and finishing processes by degrading the solubilized dye. However, laccase action must be restricted to solubilized dye molecules thereby avoiding decolorization of fabrics. Chemical modification of enzymes can provide a powerful tool to change the adsorption behaviour of enzymes on water insoluble polymers. Polyethylene glycol (PEG) was covalently attached onto a laccase from Trametes hirsuta. Different molecular weights of the synthetic polymer were tested in terms of adsorption behaviour and retained laccase activity. Covalent attachment of PEG onto the laccase resulted in enhanced enzyme stability while with increasing molecular weight of attached PEG the substrate affinity for the laccase conjugate decreased. The activity of the modified laccases on fibre bound dye was drastically reduced decreasing the adsorption of the enzyme on various fabrics. Compared to the 5 kDa PEG laccase conjugate (K/S value 47.60)SpringerUniversidade do MinhoSchroeder, M.Heumann, SonjaSilva, Carla J. S. M.Paulo, Artur CavacoGübitz, Georg M.2006-052006-05-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/12948eng0141-549210.1007/s10529-006-9052-416791729http://www.springerlink.com/content/k5651wvk08487021/info: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:RCAAP2023-07-21T12:12:50Zoai:repositorium.sdum.uminho.pt:1822/12948Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T19:04:49.941634Repositório 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 Specificities of a chemically modified laccase from trametes hirsuta on soluble and cellulose-bound substrates
title Specificities of a chemically modified laccase from trametes hirsuta on soluble and cellulose-bound substrates
spellingShingle Specificities of a chemically modified laccase from trametes hirsuta on soluble and cellulose-bound substrates
Schroeder, M.
Laccase
Polyethylene glycol
Dye-degrading
Enzyme modification
Trametes hirsuta
Science & Technology
title_short Specificities of a chemically modified laccase from trametes hirsuta on soluble and cellulose-bound substrates
title_full Specificities of a chemically modified laccase from trametes hirsuta on soluble and cellulose-bound substrates
title_fullStr Specificities of a chemically modified laccase from trametes hirsuta on soluble and cellulose-bound substrates
title_full_unstemmed Specificities of a chemically modified laccase from trametes hirsuta on soluble and cellulose-bound substrates
title_sort Specificities of a chemically modified laccase from trametes hirsuta on soluble and cellulose-bound substrates
author Schroeder, M.
author_facet Schroeder, M.
Heumann, Sonja
Silva, Carla J. S. M.
Paulo, Artur Cavaco
Gübitz, Georg M.
author_role author
author2 Heumann, Sonja
Silva, Carla J. S. M.
Paulo, Artur Cavaco
Gübitz, Georg M.
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Universidade do Minho
dc.contributor.author.fl_str_mv Schroeder, M.
Heumann, Sonja
Silva, Carla J. S. M.
Paulo, Artur Cavaco
Gübitz, Georg M.
dc.subject.por.fl_str_mv Laccase
Polyethylene glycol
Dye-degrading
Enzyme modification
Trametes hirsuta
Science & Technology
topic Laccase
Polyethylene glycol
Dye-degrading
Enzyme modification
Trametes hirsuta
Science & Technology
description Laccases could prevent fabrics and garments from re-deposition of dyes during washing and finishing processes by degrading the solubilized dye. However, laccase action must be restricted to solubilized dye molecules thereby avoiding decolorization of fabrics. Chemical modification of enzymes can provide a powerful tool to change the adsorption behaviour of enzymes on water insoluble polymers. Polyethylene glycol (PEG) was covalently attached onto a laccase from Trametes hirsuta. Different molecular weights of the synthetic polymer were tested in terms of adsorption behaviour and retained laccase activity. Covalent attachment of PEG onto the laccase resulted in enhanced enzyme stability while with increasing molecular weight of attached PEG the substrate affinity for the laccase conjugate decreased. The activity of the modified laccases on fibre bound dye was drastically reduced decreasing the adsorption of the enzyme on various fabrics. Compared to the 5 kDa PEG laccase conjugate (K/S value 47.60)
publishDate 2006
dc.date.none.fl_str_mv 2006-05
2006-05-01T00:00:00Z
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/1822/12948
url http://hdl.handle.net/1822/12948
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 0141-5492
10.1007/s10529-006-9052-4
16791729
http://www.springerlink.com/content/k5651wvk08487021/
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 Springer
publisher.none.fl_str_mv Springer
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)
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