Enzymatic polymerization on the surface of functionalized cellulose fibers
Autor(a) principal: | |
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Data de Publicação: | 2007 |
Outros Autores: | , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/1822/13817 |
Resumo: | Enzymatic coating of functionalized cellulose fibers with catechol was performed in the presence of Trametes hirsuta laccase. Cellulose functionalization was done by covalent fixation of aromatic amines onto the cellulose surface using a dyeing procedure with C.I. Reactive Black 5 (RB5) followed by reduction with sodium hydrosulfite. Cellulase enzymes were used on coated and control samples to obtain the analytes linked with the soluble sugars in solution, to prove the reaction concepts described in this paper. Hydrolyzed coated-cellulose showed lower concentration of reducing sugars (1188 mg/L) than control samples (2011 mg/L). The structures of these compounds were checked by LC/MS analysis confirming the presence of functionalized glucose and cellobiose units coupled to poly(catechol) molecules (m/z 580 and m/z 633). Alkali extraction method showed to be very promising to coat cellulose fibers with phenols in the presence of enzymes, at mild conditions of temperature and pH. |
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Enzymatic polymerization on the surface of functionalized cellulose fibersEnzymesBiopolymersRadical polymerizationCoatingsMass spectrometryScience & TechnologyEnzymatic coating of functionalized cellulose fibers with catechol was performed in the presence of Trametes hirsuta laccase. Cellulose functionalization was done by covalent fixation of aromatic amines onto the cellulose surface using a dyeing procedure with C.I. Reactive Black 5 (RB5) followed by reduction with sodium hydrosulfite. Cellulase enzymes were used on coated and control samples to obtain the analytes linked with the soluble sugars in solution, to prove the reaction concepts described in this paper. Hydrolyzed coated-cellulose showed lower concentration of reducing sugars (1188 mg/L) than control samples (2011 mg/L). The structures of these compounds were checked by LC/MS analysis confirming the presence of functionalized glucose and cellobiose units coupled to poly(catechol) molecules (m/z 580 and m/z 633). Alkali extraction method showed to be very promising to coat cellulose fibers with phenols in the presence of enzymes, at mild conditions of temperature and pH.ElsevierUniversidade do MinhoKim, SuyeonZille, AndreaMurkovic, M.Guebitz, G. M.Paulo, Artur Cavaco2007-062007-06-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/13817eng0141-022910.1016/j.enzmictec.2007.01.001http://www.sciencedirect.com/science/article/pii/S0141022907000178info: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:RCAAP2023-07-21T12:22:23Zoai:repositorium.sdum.uminho.pt:1822/13817Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T19:15:52.680342Repositório 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 polymerization on the surface of functionalized cellulose fibers |
title |
Enzymatic polymerization on the surface of functionalized cellulose fibers |
spellingShingle |
Enzymatic polymerization on the surface of functionalized cellulose fibers Kim, Suyeon Enzymes Biopolymers Radical polymerization Coatings Mass spectrometry Science & Technology |
title_short |
Enzymatic polymerization on the surface of functionalized cellulose fibers |
title_full |
Enzymatic polymerization on the surface of functionalized cellulose fibers |
title_fullStr |
Enzymatic polymerization on the surface of functionalized cellulose fibers |
title_full_unstemmed |
Enzymatic polymerization on the surface of functionalized cellulose fibers |
title_sort |
Enzymatic polymerization on the surface of functionalized cellulose fibers |
author |
Kim, Suyeon |
author_facet |
Kim, Suyeon Zille, Andrea Murkovic, M. Guebitz, G. M. Paulo, Artur Cavaco |
author_role |
author |
author2 |
Zille, Andrea Murkovic, M. Guebitz, G. M. Paulo, Artur Cavaco |
author2_role |
author author author author |
dc.contributor.none.fl_str_mv |
Universidade do Minho |
dc.contributor.author.fl_str_mv |
Kim, Suyeon Zille, Andrea Murkovic, M. Guebitz, G. M. Paulo, Artur Cavaco |
dc.subject.por.fl_str_mv |
Enzymes Biopolymers Radical polymerization Coatings Mass spectrometry Science & Technology |
topic |
Enzymes Biopolymers Radical polymerization Coatings Mass spectrometry Science & Technology |
description |
Enzymatic coating of functionalized cellulose fibers with catechol was performed in the presence of Trametes hirsuta laccase. Cellulose functionalization was done by covalent fixation of aromatic amines onto the cellulose surface using a dyeing procedure with C.I. Reactive Black 5 (RB5) followed by reduction with sodium hydrosulfite. Cellulase enzymes were used on coated and control samples to obtain the analytes linked with the soluble sugars in solution, to prove the reaction concepts described in this paper. Hydrolyzed coated-cellulose showed lower concentration of reducing sugars (1188 mg/L) than control samples (2011 mg/L). The structures of these compounds were checked by LC/MS analysis confirming the presence of functionalized glucose and cellobiose units coupled to poly(catechol) molecules (m/z 580 and m/z 633). Alkali extraction method showed to be very promising to coat cellulose fibers with phenols in the presence of enzymes, at mild conditions of temperature and pH. |
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/1822/13817 |
url |
http://hdl.handle.net/1822/13817 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
0141-0229 10.1016/j.enzmictec.2007.01.001 http://www.sciencedirect.com/science/article/pii/S0141022907000178 |
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 |
institution |
RCAAP |
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 |
repository.mail.fl_str_mv |
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1799132606447484928 |