Thermal and hydrolytic degradation of electrospun fish gelatin membranes

Detalhes bibliográficos
Autor(a) principal: Correia, D.M.
Data de Publicação: 2013
Outros Autores: Padrão, J, Rodrigues, L. R., Dourado, F., Lanceros-Mendez, S., Sencadas, V.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/11110/287
Resumo: The thermal and hydrolytic degradation of electrospun gelatin membranes cross-linked with glutaraldehyde in vapor phase has been studied. In vitro degradation of gelatin membranes was evaluated in phosphate buffer saline solution at 37 ºC. After 15 days under these conditions, a weight loss of 68 % was observed, attributed to solvation and depolymerization of the main polymeric chains. Thermal degradation kinetics of the gelatin raw material and as-spun electrospun membranes showed that the electrospinning processing conditions do not influence polymer degradation. However, for cross-linked samples a decrease in the activation energy was observed, associated with the effect of glutaraldehyde cross-linking reaction in the inter- and intra-molecular hydrogen bonds of the protein. It is also shown that the electrospinning process does not affect the formation of the helical structure of gelatin chains.
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spelling Thermal and hydrolytic degradation of electrospun fish gelatin membranesFish gelatinElectrospun membranesThermal degradationHydrolytic degradationBiomaterialsThe thermal and hydrolytic degradation of electrospun gelatin membranes cross-linked with glutaraldehyde in vapor phase has been studied. In vitro degradation of gelatin membranes was evaluated in phosphate buffer saline solution at 37 ºC. After 15 days under these conditions, a weight loss of 68 % was observed, attributed to solvation and depolymerization of the main polymeric chains. Thermal degradation kinetics of the gelatin raw material and as-spun electrospun membranes showed that the electrospinning processing conditions do not influence polymer degradation. However, for cross-linked samples a decrease in the activation energy was observed, associated with the effect of glutaraldehyde cross-linking reaction in the inter- and intra-molecular hydrogen bonds of the protein. It is also shown that the electrospinning process does not affect the formation of the helical structure of gelatin chains.This work was supported by FEDER through the COMPETE Program and by the Portuguese Foundation for Science and Technology (FCT) in the framework of the Strategic Project PEST-C/FIS/UI607/2011 and by projects project references NANO/NMed-SD/0156/2007 and PTDC/CTM-NAN/112574/2009. The authors also thank support from the COST Action MP1003, 2010 ‘European Scientific Network for Artificial Muscles’. DMC, JP and VS would like to acknowledge the FCT for the SFRH/BD/ 82411/2011, SFRH/BD/64901/2009 and SFRH/BD/64901/2009 grants respectively.2013-06-25T09:09:54Z2013-06-25T09:09:54Z2013-06-25T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://hdl.handle.net/11110/287oai:ciencipca.ipca.pt:11110/287enghttp://hdl.handle.net/11110/287Correia, D.M.Padrão, JRodrigues, L. R.Dourado, F.Lanceros-Mendez, S.Sencadas, V.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:RCAAP2022-09-05T12:51:51Zoai:ciencipca.ipca.pt:11110/287Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T15:00:41.644980Repositório 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 Thermal and hydrolytic degradation of electrospun fish gelatin membranes
title Thermal and hydrolytic degradation of electrospun fish gelatin membranes
spellingShingle Thermal and hydrolytic degradation of electrospun fish gelatin membranes
Correia, D.M.
Fish gelatin
Electrospun membranes
Thermal degradation
Hydrolytic degradation
Biomaterials
title_short Thermal and hydrolytic degradation of electrospun fish gelatin membranes
title_full Thermal and hydrolytic degradation of electrospun fish gelatin membranes
title_fullStr Thermal and hydrolytic degradation of electrospun fish gelatin membranes
title_full_unstemmed Thermal and hydrolytic degradation of electrospun fish gelatin membranes
title_sort Thermal and hydrolytic degradation of electrospun fish gelatin membranes
author Correia, D.M.
author_facet Correia, D.M.
Padrão, J
Rodrigues, L. R.
Dourado, F.
Lanceros-Mendez, S.
Sencadas, V.
author_role author
author2 Padrão, J
Rodrigues, L. R.
Dourado, F.
Lanceros-Mendez, S.
Sencadas, V.
author2_role author
author
author
author
author
dc.contributor.author.fl_str_mv Correia, D.M.
Padrão, J
Rodrigues, L. R.
Dourado, F.
Lanceros-Mendez, S.
Sencadas, V.
dc.subject.por.fl_str_mv Fish gelatin
Electrospun membranes
Thermal degradation
Hydrolytic degradation
Biomaterials
topic Fish gelatin
Electrospun membranes
Thermal degradation
Hydrolytic degradation
Biomaterials
description The thermal and hydrolytic degradation of electrospun gelatin membranes cross-linked with glutaraldehyde in vapor phase has been studied. In vitro degradation of gelatin membranes was evaluated in phosphate buffer saline solution at 37 ºC. After 15 days under these conditions, a weight loss of 68 % was observed, attributed to solvation and depolymerization of the main polymeric chains. Thermal degradation kinetics of the gelatin raw material and as-spun electrospun membranes showed that the electrospinning processing conditions do not influence polymer degradation. However, for cross-linked samples a decrease in the activation energy was observed, associated with the effect of glutaraldehyde cross-linking reaction in the inter- and intra-molecular hydrogen bonds of the protein. It is also shown that the electrospinning process does not affect the formation of the helical structure of gelatin chains.
publishDate 2013
dc.date.none.fl_str_mv 2013-06-25T09:09:54Z
2013-06-25T09:09:54Z
2013-06-25T00:00:00Z
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dc.identifier.uri.fl_str_mv http://hdl.handle.net/11110/287
oai:ciencipca.ipca.pt:11110/287
url http://hdl.handle.net/11110/287
identifier_str_mv oai:ciencipca.ipca.pt:11110/287
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv http://hdl.handle.net/11110/287
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