Effects of electric fields on protein unfolding and aggregation : Influence on edible films formation

Detalhes bibliográficos
Autor(a) principal: Pereira, Ricardo
Data de Publicação: 2010
Outros Autores: Souza, B. W. S., Cerqueira, M. A., Teixeira, J. A., Vicente, A. A.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/1822/11278
Resumo: Electric fields application is receiving increased attention because of its uniform heating of liquids. The mechanisms of unfolding and aggregation of whey proteins during ohmic heating may influence properties of edible films made thereof. The aim of this work was to evaluate the effects of ohmic heating on physical and structural properties of whey protein edible films and compare them with those obtained by conventional heating. The results showed that ohmic heating determined less aggregation and lower concentration of free sulphydryls in film-forming solutions. Ohmic films were thinner, less permeable to water vapor and presented nearly the same mechanical properties of conventional films. Ohmic heating induced protein conformational changes by increasing the contents of -sheet structures in the film network. This work emphasized the effects of ohmic heating in unfolding and aggregation mechanisms of whey proteins during heat denaturation, which determined the production of protein edible films with distinctive properties.
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spelling Effects of electric fields on protein unfolding and aggregation : Influence on edible films formationScience & TechnologyElectric fields application is receiving increased attention because of its uniform heating of liquids. The mechanisms of unfolding and aggregation of whey proteins during ohmic heating may influence properties of edible films made thereof. The aim of this work was to evaluate the effects of ohmic heating on physical and structural properties of whey protein edible films and compare them with those obtained by conventional heating. The results showed that ohmic heating determined less aggregation and lower concentration of free sulphydryls in film-forming solutions. Ohmic films were thinner, less permeable to water vapor and presented nearly the same mechanical properties of conventional films. Ohmic heating induced protein conformational changes by increasing the contents of -sheet structures in the film network. This work emphasized the effects of ohmic heating in unfolding and aggregation mechanisms of whey proteins during heat denaturation, which determined the production of protein edible films with distinctive properties.Fundação para a Ciência e Tecnologia (FCT)Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES, Brazil)American Chemical SocietyUniversidade do MinhoPereira, RicardoSouza, B. W. S.Cerqueira, M. A.Teixeira, J. A.Vicente, A. A.2010-112010-11-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/11278eng"Biomacromolecules". ISSN 1525-7797. 11:11 (Nov. 2010) 2912-2918.1525-779710.1021/bm100681a20873858info: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:RCAAP2023-07-21T12:23:22ZPortal AgregadorONG
dc.title.none.fl_str_mv Effects of electric fields on protein unfolding and aggregation : Influence on edible films formation
title Effects of electric fields on protein unfolding and aggregation : Influence on edible films formation
spellingShingle Effects of electric fields on protein unfolding and aggregation : Influence on edible films formation
Pereira, Ricardo
Science & Technology
title_short Effects of electric fields on protein unfolding and aggregation : Influence on edible films formation
title_full Effects of electric fields on protein unfolding and aggregation : Influence on edible films formation
title_fullStr Effects of electric fields on protein unfolding and aggregation : Influence on edible films formation
title_full_unstemmed Effects of electric fields on protein unfolding and aggregation : Influence on edible films formation
title_sort Effects of electric fields on protein unfolding and aggregation : Influence on edible films formation
author Pereira, Ricardo
author_facet Pereira, Ricardo
Souza, B. W. S.
Cerqueira, M. A.
Teixeira, J. A.
Vicente, A. A.
author_role author
author2 Souza, B. W. S.
Cerqueira, M. A.
Teixeira, J. A.
Vicente, A. A.
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Universidade do Minho
dc.contributor.author.fl_str_mv Pereira, Ricardo
Souza, B. W. S.
Cerqueira, M. A.
Teixeira, J. A.
Vicente, A. A.
dc.subject.por.fl_str_mv Science & Technology
topic Science & Technology
description Electric fields application is receiving increased attention because of its uniform heating of liquids. The mechanisms of unfolding and aggregation of whey proteins during ohmic heating may influence properties of edible films made thereof. The aim of this work was to evaluate the effects of ohmic heating on physical and structural properties of whey protein edible films and compare them with those obtained by conventional heating. The results showed that ohmic heating determined less aggregation and lower concentration of free sulphydryls in film-forming solutions. Ohmic films were thinner, less permeable to water vapor and presented nearly the same mechanical properties of conventional films. Ohmic heating induced protein conformational changes by increasing the contents of -sheet structures in the film network. This work emphasized the effects of ohmic heating in unfolding and aggregation mechanisms of whey proteins during heat denaturation, which determined the production of protein edible films with distinctive properties.
publishDate 2010
dc.date.none.fl_str_mv 2010-11
2010-11-01T00:00:00Z
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/1822/11278
url http://hdl.handle.net/1822/11278
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv "Biomacromolecules". ISSN 1525-7797. 11:11 (Nov. 2010) 2912-2918.
1525-7797
10.1021/bm100681a
20873858
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 American Chemical Society
publisher.none.fl_str_mv American Chemical Society
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
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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)
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