Interactions of cotton with CBD peptides
Autor(a) principal: | |
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Data de Publicação: | 1999 |
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/1822/2403 |
Resumo: | The binding of genetically engineered Family II cellulose binding domains (CBDs) of Cellumonas fimi cellulases to cotton fabrics was studied and possible textile applications were investigated. Family II CBDs bound to cotton cellulose increased dye affinity, especially for acid dyes, but with very poor washing fastness. Ironing of the protein bound fabrics before dyeing increases dye affinity, which is probably due to protein denaturation and thus increases exposition of ionic groups. For desorption of CBD proteins from the cotton fabric, high levels of mechanical agitation and alkaline conditions (pH >7) are necessary. Binding of Family II CBDs to cellulose releases fine particles, whereas migration and desorption did not. Long time storage of cotton fabrics with adsorbed CBD proteins did not cause changes in their physical properties and did not damage cotton cellulose. The presence of water on the surface of cellulose was found to be essential for the interfabric migration of Family II CBDs. The double binding cellulose domain binds strongly on cotton and their interfabric migration is smaller. (C) 1999 Elsevier Science Inc. All rights reserved. |
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Interactions of cotton with CBD peptidescellulasesadsorptioncellulose binding domain (CBD)cottonScience & TechnologyThe binding of genetically engineered Family II cellulose binding domains (CBDs) of Cellumonas fimi cellulases to cotton fabrics was studied and possible textile applications were investigated. Family II CBDs bound to cotton cellulose increased dye affinity, especially for acid dyes, but with very poor washing fastness. Ironing of the protein bound fabrics before dyeing increases dye affinity, which is probably due to protein denaturation and thus increases exposition of ionic groups. For desorption of CBD proteins from the cotton fabric, high levels of mechanical agitation and alkaline conditions (pH >7) are necessary. Binding of Family II CBDs to cellulose releases fine particles, whereas migration and desorption did not. Long time storage of cotton fabrics with adsorbed CBD proteins did not cause changes in their physical properties and did not damage cotton cellulose. The presence of water on the surface of cellulose was found to be essential for the interfabric migration of Family II CBDs. The double binding cellulose domain binds strongly on cotton and their interfabric migration is smaller. (C) 1999 Elsevier Science Inc. All rights reserved.ElsevierUniversidade do MinhoPaulo, Artur CavacoMorgado, JoséAndreaus, JuergenKilburn, Douglas19991999-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/2403eng"Enzyme and microbial technology". ISSN 0141-0229. 25:8-9 (Nov. 1999) 639-672.0141-022910.1016/S0141-0229(99)00101-5info: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:RCAAP2023-07-21T12:40:01Zoai:repositorium.sdum.uminho.pt:1822/2403Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T19:36:45.374778Repositório 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 |
Interactions of cotton with CBD peptides |
title |
Interactions of cotton with CBD peptides |
spellingShingle |
Interactions of cotton with CBD peptides Paulo, Artur Cavaco cellulases adsorption cellulose binding domain (CBD) cotton Science & Technology |
title_short |
Interactions of cotton with CBD peptides |
title_full |
Interactions of cotton with CBD peptides |
title_fullStr |
Interactions of cotton with CBD peptides |
title_full_unstemmed |
Interactions of cotton with CBD peptides |
title_sort |
Interactions of cotton with CBD peptides |
author |
Paulo, Artur Cavaco |
author_facet |
Paulo, Artur Cavaco Morgado, José Andreaus, Juergen Kilburn, Douglas |
author_role |
author |
author2 |
Morgado, José Andreaus, Juergen Kilburn, Douglas |
author2_role |
author author author |
dc.contributor.none.fl_str_mv |
Universidade do Minho |
dc.contributor.author.fl_str_mv |
Paulo, Artur Cavaco Morgado, José Andreaus, Juergen Kilburn, Douglas |
dc.subject.por.fl_str_mv |
cellulases adsorption cellulose binding domain (CBD) cotton Science & Technology |
topic |
cellulases adsorption cellulose binding domain (CBD) cotton Science & Technology |
description |
The binding of genetically engineered Family II cellulose binding domains (CBDs) of Cellumonas fimi cellulases to cotton fabrics was studied and possible textile applications were investigated. Family II CBDs bound to cotton cellulose increased dye affinity, especially for acid dyes, but with very poor washing fastness. Ironing of the protein bound fabrics before dyeing increases dye affinity, which is probably due to protein denaturation and thus increases exposition of ionic groups. For desorption of CBD proteins from the cotton fabric, high levels of mechanical agitation and alkaline conditions (pH >7) are necessary. Binding of Family II CBDs to cellulose releases fine particles, whereas migration and desorption did not. Long time storage of cotton fabrics with adsorbed CBD proteins did not cause changes in their physical properties and did not damage cotton cellulose. The presence of water on the surface of cellulose was found to be essential for the interfabric migration of Family II CBDs. The double binding cellulose domain binds strongly on cotton and their interfabric migration is smaller. (C) 1999 Elsevier Science Inc. All rights reserved. |
publishDate |
1999 |
dc.date.none.fl_str_mv |
1999 1999-01-01T00:00:00Z |
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/1822/2403 |
url |
http://hdl.handle.net/1822/2403 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
"Enzyme and microbial technology". ISSN 0141-0229. 25:8-9 (Nov. 1999) 639-672. 0141-0229 10.1016/S0141-0229(99)00101-5 |
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 |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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RCAAP |
institution |
RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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1799132897630748672 |