Accessing gelling ability of vegetable proteins using rheological and fluorescence techniques
Autor(a) principal: | |
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Data de Publicação: | 2005 |
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/10400.5/2419 |
Resumo: | This work aims to present a comprehensive study about the macroscopic characteristics of globular vegetable proteins, in terms of their gelling ability, by understanding their molecular behaviour, when submitted to a thermal gelling process. The gels of soy, pea and lupin proteins were characterized by rheological techniques. Gelation kinetics, mechanical spectra, as well as the texture of these gels were analyzed and compared. Additionally, capillary viscometry, steady-state fluorescence and fluorescence anisotropy were used to monitor the structural changes induced by the thermal denaturation, which constitutes the main condition for the formation of a gel structure. Based on these techniques it was possible to establish a relationship between the gelling ability of each protein isolate and their structural resistance to thermal unfolding, enabling us to explain the weakest and the strongest gelling ability observed for lupin and soy proteins isolates, respectively |
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spelling |
Accessing gelling ability of vegetable proteins using rheological and fluorescence techniquesvegetable proteinsgelsintrinsic viscosityrheologysteady-state fluorescencefluorescence anisotropyThis work aims to present a comprehensive study about the macroscopic characteristics of globular vegetable proteins, in terms of their gelling ability, by understanding their molecular behaviour, when submitted to a thermal gelling process. The gels of soy, pea and lupin proteins were characterized by rheological techniques. Gelation kinetics, mechanical spectra, as well as the texture of these gels were analyzed and compared. Additionally, capillary viscometry, steady-state fluorescence and fluorescence anisotropy were used to monitor the structural changes induced by the thermal denaturation, which constitutes the main condition for the formation of a gel structure. Based on these techniques it was possible to establish a relationship between the gelling ability of each protein isolate and their structural resistance to thermal unfolding, enabling us to explain the weakest and the strongest gelling ability observed for lupin and soy proteins isolates, respectivelyElsevierRepositório da Universidade de LisboaSousa, IsabelBatista, Ana PaulaPortugal, Carla A.M.Crespo, João G.Raymundo, Anabela2010-10-28T15:39:01Z20052005-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.5/2419eng"International Journal of Biological Macromolecules". ISSN 0141-8130. 36 (2005) 135-1430141-8130info: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:RCAAP2023-03-06T14:33:37Zoai:www.repository.utl.pt:10400.5/2419Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T16:50:25.477324Repositório 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 |
Accessing gelling ability of vegetable proteins using rheological and fluorescence techniques |
title |
Accessing gelling ability of vegetable proteins using rheological and fluorescence techniques |
spellingShingle |
Accessing gelling ability of vegetable proteins using rheological and fluorescence techniques Sousa, Isabel vegetable proteins gels intrinsic viscosity rheology steady-state fluorescence fluorescence anisotropy |
title_short |
Accessing gelling ability of vegetable proteins using rheological and fluorescence techniques |
title_full |
Accessing gelling ability of vegetable proteins using rheological and fluorescence techniques |
title_fullStr |
Accessing gelling ability of vegetable proteins using rheological and fluorescence techniques |
title_full_unstemmed |
Accessing gelling ability of vegetable proteins using rheological and fluorescence techniques |
title_sort |
Accessing gelling ability of vegetable proteins using rheological and fluorescence techniques |
author |
Sousa, Isabel |
author_facet |
Sousa, Isabel Batista, Ana Paula Portugal, Carla A.M. Crespo, João G. Raymundo, Anabela |
author_role |
author |
author2 |
Batista, Ana Paula Portugal, Carla A.M. Crespo, João G. Raymundo, Anabela |
author2_role |
author author author author |
dc.contributor.none.fl_str_mv |
Repositório da Universidade de Lisboa |
dc.contributor.author.fl_str_mv |
Sousa, Isabel Batista, Ana Paula Portugal, Carla A.M. Crespo, João G. Raymundo, Anabela |
dc.subject.por.fl_str_mv |
vegetable proteins gels intrinsic viscosity rheology steady-state fluorescence fluorescence anisotropy |
topic |
vegetable proteins gels intrinsic viscosity rheology steady-state fluorescence fluorescence anisotropy |
description |
This work aims to present a comprehensive study about the macroscopic characteristics of globular vegetable proteins, in terms of their gelling ability, by understanding their molecular behaviour, when submitted to a thermal gelling process. The gels of soy, pea and lupin proteins were characterized by rheological techniques. Gelation kinetics, mechanical spectra, as well as the texture of these gels were analyzed and compared. Additionally, capillary viscometry, steady-state fluorescence and fluorescence anisotropy were used to monitor the structural changes induced by the thermal denaturation, which constitutes the main condition for the formation of a gel structure. Based on these techniques it was possible to establish a relationship between the gelling ability of each protein isolate and their structural resistance to thermal unfolding, enabling us to explain the weakest and the strongest gelling ability observed for lupin and soy proteins isolates, respectively |
publishDate |
2005 |
dc.date.none.fl_str_mv |
2005 2005-01-01T00:00:00Z 2010-10-28T15:39:01Z |
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/10400.5/2419 |
url |
http://hdl.handle.net/10400.5/2419 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
"International Journal of Biological Macromolecules". ISSN 0141-8130. 36 (2005) 135-143 0141-8130 |
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 |
repository.mail.fl_str_mv |
|
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1799130979329114112 |