Large-scale production of cellulose-binding domains : adsorption studies using CBD-FITC conjugates

Detalhes bibliográficos
Autor(a) principal: Pinto, João Ricardo
Data de Publicação: 2006
Outros Autores: Carvalho, Joana, Mota, M., Gama, F. 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/1822/5498
Resumo: A method for the gram-scale production of cellulose-binding domains (CBD) through the proteolytic digestion of a commercial nzymatic preparation (Celluclast) was developed. The CBD obtained, isolated from Trichoderma reesei cellobiohydrolase I, is highly pure and heavily glycosylated. The purified peptide has a molecular weight of 8.43 kDa, comprising the binding module, a part of the linker, and about 30% glycosidic moiety. Its properties may thus be different from recombinant ones expressed in bacteria. CBDfluorescein isothiocyanate conjugates were used to study the CBD-cellulose interaction. The presence of fluorescent peptides adsorbed on crystalline and amorphous cellulose fibers suggests that amorphous regions have a higher concentration of binding sites. The adsorption is reversible, but desorption is a very slow process.
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spelling Large-scale production of cellulose-binding domains : adsorption studies using CBD-FITC conjugatesAdsorptionCellulose-binding domainsFITCProteolysisScience & TechnologyA method for the gram-scale production of cellulose-binding domains (CBD) through the proteolytic digestion of a commercial nzymatic preparation (Celluclast) was developed. The CBD obtained, isolated from Trichoderma reesei cellobiohydrolase I, is highly pure and heavily glycosylated. The purified peptide has a molecular weight of 8.43 kDa, comprising the binding module, a part of the linker, and about 30% glycosidic moiety. Its properties may thus be different from recombinant ones expressed in bacteria. CBDfluorescein isothiocyanate conjugates were used to study the CBD-cellulose interaction. The presence of fluorescent peptides adsorbed on crystalline and amorphous cellulose fibers suggests that amorphous regions have a higher concentration of binding sites. The adsorption is reversible, but desorption is a very slow process.Fundação para a Ciência e a Tecnologia (FCT)SpringerUniversidade do MinhoPinto, João RicardoCarvalho, JoanaMota, M.Gama, F. M.2006-102006-10-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/5498eng"Cellulose". ISSN 0969-0239. 13:5 (Oct. 2006) 557-569.0969-023910.1007/s10570-006-9060-5info: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:RCAAP2023-07-21T12:10:33Zoai:repositorium.sdum.uminho.pt:1822/5498Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T19:02:12.100430Repositório 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 Large-scale production of cellulose-binding domains : adsorption studies using CBD-FITC conjugates
title Large-scale production of cellulose-binding domains : adsorption studies using CBD-FITC conjugates
spellingShingle Large-scale production of cellulose-binding domains : adsorption studies using CBD-FITC conjugates
Pinto, João Ricardo
Adsorption
Cellulose-binding domains
FITC
Proteolysis
Science & Technology
title_short Large-scale production of cellulose-binding domains : adsorption studies using CBD-FITC conjugates
title_full Large-scale production of cellulose-binding domains : adsorption studies using CBD-FITC conjugates
title_fullStr Large-scale production of cellulose-binding domains : adsorption studies using CBD-FITC conjugates
title_full_unstemmed Large-scale production of cellulose-binding domains : adsorption studies using CBD-FITC conjugates
title_sort Large-scale production of cellulose-binding domains : adsorption studies using CBD-FITC conjugates
author Pinto, João Ricardo
author_facet Pinto, João Ricardo
Carvalho, Joana
Mota, M.
Gama, F. M.
author_role author
author2 Carvalho, Joana
Mota, M.
Gama, F. M.
author2_role author
author
author
dc.contributor.none.fl_str_mv Universidade do Minho
dc.contributor.author.fl_str_mv Pinto, João Ricardo
Carvalho, Joana
Mota, M.
Gama, F. M.
dc.subject.por.fl_str_mv Adsorption
Cellulose-binding domains
FITC
Proteolysis
Science & Technology
topic Adsorption
Cellulose-binding domains
FITC
Proteolysis
Science & Technology
description A method for the gram-scale production of cellulose-binding domains (CBD) through the proteolytic digestion of a commercial nzymatic preparation (Celluclast) was developed. The CBD obtained, isolated from Trichoderma reesei cellobiohydrolase I, is highly pure and heavily glycosylated. The purified peptide has a molecular weight of 8.43 kDa, comprising the binding module, a part of the linker, and about 30% glycosidic moiety. Its properties may thus be different from recombinant ones expressed in bacteria. CBDfluorescein isothiocyanate conjugates were used to study the CBD-cellulose interaction. The presence of fluorescent peptides adsorbed on crystalline and amorphous cellulose fibers suggests that amorphous regions have a higher concentration of binding sites. The adsorption is reversible, but desorption is a very slow process.
publishDate 2006
dc.date.none.fl_str_mv 2006-10
2006-10-01T00:00:00Z
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/1822/5498
url http://hdl.handle.net/1822/5498
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv "Cellulose". ISSN 0969-0239. 13:5 (Oct. 2006) 557-569.
0969-0239
10.1007/s10570-006-9060-5
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 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
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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