Studies on the properties of Celluclast/Eudragit L-100 conjugate

Detalhes bibliográficos
Autor(a) principal: Dourado, Fernando
Data de Publicação: 2002
Outros Autores: Bastos, Maria de Lurdes, 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/1822/1472
Resumo: A cellulase from Trichoderma reesei was immobilized on Eudragit L-100, a reversibly soluble polymer depending on the pH of the medium. The solubility of the modified cellulase was studied at different pH values. By changing the pH, the adsorption equilibrium of the derivatized proteins is switched towards the liquid phase, thus making recycling possible. This method allows for improved stability, without major loss of specific activity. The adsorption of cellulase on Eudragit lowers the enthalpy of denaturation, but affects only slightly the denaturation temperature. The use of carbodiimide was ineffective on linking the enzymes covalently to the polymer, since the immobilization process was found to be only mediated by non-covalent forces.
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spelling Studies on the properties of Celluclast/Eudragit L-100 conjugateCellulaseCarbodiimideEudragit L-100Enzyme immobilizationDSCScience & TechnologyA cellulase from Trichoderma reesei was immobilized on Eudragit L-100, a reversibly soluble polymer depending on the pH of the medium. The solubility of the modified cellulase was studied at different pH values. By changing the pH, the adsorption equilibrium of the derivatized proteins is switched towards the liquid phase, thus making recycling possible. This method allows for improved stability, without major loss of specific activity. The adsorption of cellulase on Eudragit lowers the enthalpy of denaturation, but affects only slightly the denaturation temperature. The use of carbodiimide was ineffective on linking the enzymes covalently to the polymer, since the immobilization process was found to be only mediated by non-covalent forces.INCO-DC (96-2205) - OLONOCO.ElsevierUniversidade do MinhoDourado, FernandoBastos, Maria de LurdesMota, M.Gama, F. M.20022002-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/1472eng“Journal of Biotechnology”. ISSN 0168-1656. 99:2 (2002) 121-131.0168-165610.1016/S0168-1656(02)00178-512270600info: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:RCAAP2023-07-21T12:36:49Zoai:repositorium.sdum.uminho.pt:1822/1472Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T19:32:59.657163Repositório 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 Studies on the properties of Celluclast/Eudragit L-100 conjugate
title Studies on the properties of Celluclast/Eudragit L-100 conjugate
spellingShingle Studies on the properties of Celluclast/Eudragit L-100 conjugate
Dourado, Fernando
Cellulase
Carbodiimide
Eudragit L-100
Enzyme immobilization
DSC
Science & Technology
title_short Studies on the properties of Celluclast/Eudragit L-100 conjugate
title_full Studies on the properties of Celluclast/Eudragit L-100 conjugate
title_fullStr Studies on the properties of Celluclast/Eudragit L-100 conjugate
title_full_unstemmed Studies on the properties of Celluclast/Eudragit L-100 conjugate
title_sort Studies on the properties of Celluclast/Eudragit L-100 conjugate
author Dourado, Fernando
author_facet Dourado, Fernando
Bastos, Maria de Lurdes
Mota, M.
Gama, F. M.
author_role author
author2 Bastos, Maria de Lurdes
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 Dourado, Fernando
Bastos, Maria de Lurdes
Mota, M.
Gama, F. M.
dc.subject.por.fl_str_mv Cellulase
Carbodiimide
Eudragit L-100
Enzyme immobilization
DSC
Science & Technology
topic Cellulase
Carbodiimide
Eudragit L-100
Enzyme immobilization
DSC
Science & Technology
description A cellulase from Trichoderma reesei was immobilized on Eudragit L-100, a reversibly soluble polymer depending on the pH of the medium. The solubility of the modified cellulase was studied at different pH values. By changing the pH, the adsorption equilibrium of the derivatized proteins is switched towards the liquid phase, thus making recycling possible. This method allows for improved stability, without major loss of specific activity. The adsorption of cellulase on Eudragit lowers the enthalpy of denaturation, but affects only slightly the denaturation temperature. The use of carbodiimide was ineffective on linking the enzymes covalently to the polymer, since the immobilization process was found to be only mediated by non-covalent forces.
publishDate 2002
dc.date.none.fl_str_mv 2002
2002-01-01T00:00:00Z
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/1822/1472
url http://hdl.handle.net/1822/1472
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv “Journal of Biotechnology”. ISSN 0168-1656. 99:2 (2002) 121-131.
0168-1656
10.1016/S0168-1656(02)00178-5
12270600
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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