Interactions of cotton with CBD peptides

Detalhes bibliográficos
Autor(a) principal: Paulo, Artur Cavaco
Data de Publicação: 1999
Outros Autores: Morgado, José, Andreaus, Juergen, Kilburn, Douglas
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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spelling 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
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
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