Stability studies of a recombinant cutinase immobilized to dextran and derivatized silica supports

Detalhes bibliográficos
Autor(a) principal: Gonçalves, A. M.
Data de Publicação: 1999
Outros Autores: Schacht, E., Matthijs, G., Barros, M. R. Aires, Cabral, J. M. S., Gil, M. H.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10316/3842
https://doi.org/10.1016/S0141-0229(98)00089-1
Resumo: Recombinant cutinase from Fusarium solani pisi was covalently attached to dextran and two derivatized silica supports, Biosil-NH2 and Biosil-Dextran-NH2. Kinetic parameters were determined for all three systems as well as for soluble cutinase. Long-term stability in aqueous media was studied; dextran may have a stabilizing role not only due to the covalent links involved but also in the same way as other polyhydroxides in aqueous media. Differential scanning calorimetry analysis suggests an enhancement of conformational stability of the immobilized forms.
id RCAP_d6fcb30aafae99ae8121d345720a5aba
oai_identifier_str oai:estudogeral.uc.pt:10316/3842
network_acronym_str RCAP
network_name_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository_id_str 7160
spelling Stability studies of a recombinant cutinase immobilized to dextran and derivatized silica supportsConformational stabilitycutinasedextranimmobilizationthermostabilityRecombinant cutinase from Fusarium solani pisi was covalently attached to dextran and two derivatized silica supports, Biosil-NH2 and Biosil-Dextran-NH2. Kinetic parameters were determined for all three systems as well as for soluble cutinase. Long-term stability in aqueous media was studied; dextran may have a stabilizing role not only due to the covalent links involved but also in the same way as other polyhydroxides in aqueous media. Differential scanning calorimetry analysis suggests an enhancement of conformational stability of the immobilized forms.http://www.sciencedirect.com/science/article/B6TG1-4165DGC-9/1/b62e6c1431e1ea508958b867559591981999info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleaplication/PDFhttp://hdl.handle.net/10316/3842http://hdl.handle.net/10316/3842https://doi.org/10.1016/S0141-0229(98)00089-1engEnzyme and Microbial Technology. 24:1-2 (1999) 60-66Gonçalves, A. M.Schacht, E.Matthijs, G.Barros, M. R. AiresCabral, J. M. S.Gil, M. H.info: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:RCAAP2021-07-20T10:29:42Zoai:estudogeral.uc.pt:10316/3842Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T20:59:16.834514Repositório 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 Stability studies of a recombinant cutinase immobilized to dextran and derivatized silica supports
title Stability studies of a recombinant cutinase immobilized to dextran and derivatized silica supports
spellingShingle Stability studies of a recombinant cutinase immobilized to dextran and derivatized silica supports
Gonçalves, A. M.
Conformational stability
cutinase
dextran
immobilization
thermostability
title_short Stability studies of a recombinant cutinase immobilized to dextran and derivatized silica supports
title_full Stability studies of a recombinant cutinase immobilized to dextran and derivatized silica supports
title_fullStr Stability studies of a recombinant cutinase immobilized to dextran and derivatized silica supports
title_full_unstemmed Stability studies of a recombinant cutinase immobilized to dextran and derivatized silica supports
title_sort Stability studies of a recombinant cutinase immobilized to dextran and derivatized silica supports
author Gonçalves, A. M.
author_facet Gonçalves, A. M.
Schacht, E.
Matthijs, G.
Barros, M. R. Aires
Cabral, J. M. S.
Gil, M. H.
author_role author
author2 Schacht, E.
Matthijs, G.
Barros, M. R. Aires
Cabral, J. M. S.
Gil, M. H.
author2_role author
author
author
author
author
dc.contributor.author.fl_str_mv Gonçalves, A. M.
Schacht, E.
Matthijs, G.
Barros, M. R. Aires
Cabral, J. M. S.
Gil, M. H.
dc.subject.por.fl_str_mv Conformational stability
cutinase
dextran
immobilization
thermostability
topic Conformational stability
cutinase
dextran
immobilization
thermostability
description Recombinant cutinase from Fusarium solani pisi was covalently attached to dextran and two derivatized silica supports, Biosil-NH2 and Biosil-Dextran-NH2. Kinetic parameters were determined for all three systems as well as for soluble cutinase. Long-term stability in aqueous media was studied; dextran may have a stabilizing role not only due to the covalent links involved but also in the same way as other polyhydroxides in aqueous media. Differential scanning calorimetry analysis suggests an enhancement of conformational stability of the immobilized forms.
publishDate 1999
dc.date.none.fl_str_mv 1999
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/10316/3842
http://hdl.handle.net/10316/3842
https://doi.org/10.1016/S0141-0229(98)00089-1
url http://hdl.handle.net/10316/3842
https://doi.org/10.1016/S0141-0229(98)00089-1
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Enzyme and Microbial Technology. 24:1-2 (1999) 60-66
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv aplication/PDF
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
_version_ 1799133884101689344

Registros relacionados