Study of the thermal stability and enzymatic activity of an immobilised enzymatic system for the bilirubin oxidation
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/10316/3840 https://doi.org/10.1016/S0142-9612(98)00228-2 |
Resumo: | In this work, we have studied the immobilisation of the haemoglobin/glucose oxidase coupled enzymatic system in poly(vinyl alcohol) membranes. These are to be used as a reagent phase either in the development of an optical sensor or as an efficient bilirubin (BR) removal reactor. Poly(vinyl alcohol) (PVA) was chosen as the support for this purpose, due to its good biocompatibility, hydrophilicity and non-thrombogenic effects. A hydrogel containing the enzymatic system, consisting of PVA crosslinked with glutaraldehyde, was prepared and characterised by DSC, enzyme activity measurements and release tests. Investigating protein conformational changes as a function of temperature and the enzymatic system activity we have found that, in spite of the destabilizing effect of the glutaraldehyde in the acidic medium, the PVA insolubilisation conditions seem do not perturb either the conformation of the [`]native state' nor the enzymatic system activity. Moreover, it was found that PVA/glutaraldehyde membranes offer a simple way to hold enzymatic system, with the possibility of controlling the conditions to obtain either the effective prevention of leaching of the entrapped proteins or the in situ delivery of the haemoglobin. |
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Study of the thermal stability and enzymatic activity of an immobilised enzymatic system for the bilirubin oxidationBilirubinHaemoglobinGlucose oxidasePoly(vinyl alcohol)Differential scanning calorimetry (DSC)In this work, we have studied the immobilisation of the haemoglobin/glucose oxidase coupled enzymatic system in poly(vinyl alcohol) membranes. These are to be used as a reagent phase either in the development of an optical sensor or as an efficient bilirubin (BR) removal reactor. Poly(vinyl alcohol) (PVA) was chosen as the support for this purpose, due to its good biocompatibility, hydrophilicity and non-thrombogenic effects. A hydrogel containing the enzymatic system, consisting of PVA crosslinked with glutaraldehyde, was prepared and characterised by DSC, enzyme activity measurements and release tests. Investigating protein conformational changes as a function of temperature and the enzymatic system activity we have found that, in spite of the destabilizing effect of the glutaraldehyde in the acidic medium, the PVA insolubilisation conditions seem do not perturb either the conformation of the [`]native state' nor the enzymatic system activity. Moreover, it was found that PVA/glutaraldehyde membranes offer a simple way to hold enzymatic system, with the possibility of controlling the conditions to obtain either the effective prevention of leaching of the entrapped proteins or the in situ delivery of the haemoglobin.http://www.sciencedirect.com/science/article/B6TWB-3WN7BVW-6/1/e0eaa7d95e2a3cd559b85f445644c3871999info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleaplication/PDFhttp://hdl.handle.net/10316/3840http://hdl.handle.net/10316/3840https://doi.org/10.1016/S0142-9612(98)00228-2engBiomaterials. 20:8 (1999) 757-763Vidal, M. M.Gil, M. H.Delgadillo, I.Alonso, J.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:RCAAP2020-11-06T16:59:36Zoai:estudogeral.uc.pt:10316/3840Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T20:59:16.785950Repositório 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 |
Study of the thermal stability and enzymatic activity of an immobilised enzymatic system for the bilirubin oxidation |
title |
Study of the thermal stability and enzymatic activity of an immobilised enzymatic system for the bilirubin oxidation |
spellingShingle |
Study of the thermal stability and enzymatic activity of an immobilised enzymatic system for the bilirubin oxidation Vidal, M. M. Bilirubin Haemoglobin Glucose oxidase Poly(vinyl alcohol) Differential scanning calorimetry (DSC) |
title_short |
Study of the thermal stability and enzymatic activity of an immobilised enzymatic system for the bilirubin oxidation |
title_full |
Study of the thermal stability and enzymatic activity of an immobilised enzymatic system for the bilirubin oxidation |
title_fullStr |
Study of the thermal stability and enzymatic activity of an immobilised enzymatic system for the bilirubin oxidation |
title_full_unstemmed |
Study of the thermal stability and enzymatic activity of an immobilised enzymatic system for the bilirubin oxidation |
title_sort |
Study of the thermal stability and enzymatic activity of an immobilised enzymatic system for the bilirubin oxidation |
author |
Vidal, M. M. |
author_facet |
Vidal, M. M. Gil, M. H. Delgadillo, I. Alonso, J. |
author_role |
author |
author2 |
Gil, M. H. Delgadillo, I. Alonso, J. |
author2_role |
author author author |
dc.contributor.author.fl_str_mv |
Vidal, M. M. Gil, M. H. Delgadillo, I. Alonso, J. |
dc.subject.por.fl_str_mv |
Bilirubin Haemoglobin Glucose oxidase Poly(vinyl alcohol) Differential scanning calorimetry (DSC) |
topic |
Bilirubin Haemoglobin Glucose oxidase Poly(vinyl alcohol) Differential scanning calorimetry (DSC) |
description |
In this work, we have studied the immobilisation of the haemoglobin/glucose oxidase coupled enzymatic system in poly(vinyl alcohol) membranes. These are to be used as a reagent phase either in the development of an optical sensor or as an efficient bilirubin (BR) removal reactor. Poly(vinyl alcohol) (PVA) was chosen as the support for this purpose, due to its good biocompatibility, hydrophilicity and non-thrombogenic effects. A hydrogel containing the enzymatic system, consisting of PVA crosslinked with glutaraldehyde, was prepared and characterised by DSC, enzyme activity measurements and release tests. Investigating protein conformational changes as a function of temperature and the enzymatic system activity we have found that, in spite of the destabilizing effect of the glutaraldehyde in the acidic medium, the PVA insolubilisation conditions seem do not perturb either the conformation of the [`]native state' nor the enzymatic system activity. Moreover, it was found that PVA/glutaraldehyde membranes offer a simple way to hold enzymatic system, with the possibility of controlling the conditions to obtain either the effective prevention of leaching of the entrapped proteins or the in situ delivery of the haemoglobin. |
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/10316/3840 http://hdl.handle.net/10316/3840 https://doi.org/10.1016/S0142-9612(98)00228-2 |
url |
http://hdl.handle.net/10316/3840 https://doi.org/10.1016/S0142-9612(98)00228-2 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Biomaterials. 20:8 (1999) 757-763 |
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 |
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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) |
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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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1799133884099592192 |