Thermal studies on protein isolates of white lupin seeds (Lupinus albus).
Autor(a) principal: | |
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Data de Publicação: | 2011 |
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/10174/3428 https://doi.org/10.1007/s10973-011-1898-6 |
Resumo: | This study used TG, DSC, and SDS-PAGE techniques to study protein isolates (PIs) in the powder form obtained from lupin seeds flour Lupinus albus. Different methods of preparing PIs were tested, resulting in final products that were different only in relation to the yield and protein content. The results of the protein analysis by SDS-PAGE showed that the same protein fractions were present in the lupin seeds and in the obtained PIs. This result shows that the process of extraction was not damaging to the composition of the original protein. On the other hand, the results of the thermal analysis (DSC and TG–DTG curves) obtained for the different PIs, led to the detection of changes in the protein conformation through the ΔH values, which in general decreased with increasing values of pH and ionic strength in the experimental conditions of extraction. Keywords Lupinus albus, TG, DSC, Protein isolate, SDS-PAGE |
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Thermal studies on protein isolates of white lupin seeds (Lupinus albus).Lupinus albusTGDSCProtein isolateSDS-PAGEThis study used TG, DSC, and SDS-PAGE techniques to study protein isolates (PIs) in the powder form obtained from lupin seeds flour Lupinus albus. Different methods of preparing PIs were tested, resulting in final products that were different only in relation to the yield and protein content. The results of the protein analysis by SDS-PAGE showed that the same protein fractions were present in the lupin seeds and in the obtained PIs. This result shows that the process of extraction was not damaging to the composition of the original protein. On the other hand, the results of the thermal analysis (DSC and TG–DTG curves) obtained for the different PIs, led to the detection of changes in the protein conformation through the ΔH values, which in general decreased with increasing values of pH and ionic strength in the experimental conditions of extraction. Keywords Lupinus albus, TG, DSC, Protein isolate, SDS-PAGEJournal of Thermal Analysis and Calorimetry2012-01-12T11:44:58Z2012-01-122011-09-24T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://hdl.handle.net/10174/3428http://hdl.handle.net/10174/3428https://doi.org/10.1007/s10973-011-1898-6engICAAMgufontanari@gmail.comjmartins@uevora.ptndndndndndFontanari, G.G.Martins, J.M.Kobelnik, M.Pastre, I.A.Arêas, J.A.G.Batistuti, J.P.Fertonani, F.L.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:RCAAP2024-01-03T18:40:36Zoai:dspace.uevora.pt:10174/3428Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T00:58:52.679839Repositório 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 studies on protein isolates of white lupin seeds (Lupinus albus). |
title |
Thermal studies on protein isolates of white lupin seeds (Lupinus albus). |
spellingShingle |
Thermal studies on protein isolates of white lupin seeds (Lupinus albus). Fontanari, G.G. Lupinus albus TG DSC Protein isolate SDS-PAGE |
title_short |
Thermal studies on protein isolates of white lupin seeds (Lupinus albus). |
title_full |
Thermal studies on protein isolates of white lupin seeds (Lupinus albus). |
title_fullStr |
Thermal studies on protein isolates of white lupin seeds (Lupinus albus). |
title_full_unstemmed |
Thermal studies on protein isolates of white lupin seeds (Lupinus albus). |
title_sort |
Thermal studies on protein isolates of white lupin seeds (Lupinus albus). |
author |
Fontanari, G.G. |
author_facet |
Fontanari, G.G. Martins, J.M. Kobelnik, M. Pastre, I.A. Arêas, J.A.G. Batistuti, J.P. Fertonani, F.L. |
author_role |
author |
author2 |
Martins, J.M. Kobelnik, M. Pastre, I.A. Arêas, J.A.G. Batistuti, J.P. Fertonani, F.L. |
author2_role |
author author author author author author |
dc.contributor.author.fl_str_mv |
Fontanari, G.G. Martins, J.M. Kobelnik, M. Pastre, I.A. Arêas, J.A.G. Batistuti, J.P. Fertonani, F.L. |
dc.subject.por.fl_str_mv |
Lupinus albus TG DSC Protein isolate SDS-PAGE |
topic |
Lupinus albus TG DSC Protein isolate SDS-PAGE |
description |
This study used TG, DSC, and SDS-PAGE techniques to study protein isolates (PIs) in the powder form obtained from lupin seeds flour Lupinus albus. Different methods of preparing PIs were tested, resulting in final products that were different only in relation to the yield and protein content. The results of the protein analysis by SDS-PAGE showed that the same protein fractions were present in the lupin seeds and in the obtained PIs. This result shows that the process of extraction was not damaging to the composition of the original protein. On the other hand, the results of the thermal analysis (DSC and TG–DTG curves) obtained for the different PIs, led to the detection of changes in the protein conformation through the ΔH values, which in general decreased with increasing values of pH and ionic strength in the experimental conditions of extraction. Keywords Lupinus albus, TG, DSC, Protein isolate, SDS-PAGE |
publishDate |
2011 |
dc.date.none.fl_str_mv |
2011-09-24T00:00:00Z 2012-01-12T11:44:58Z 2012-01-12 |
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/10174/3428 http://hdl.handle.net/10174/3428 https://doi.org/10.1007/s10973-011-1898-6 |
url |
http://hdl.handle.net/10174/3428 https://doi.org/10.1007/s10973-011-1898-6 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
ICAAM gufontanari@gmail.com jmartins@uevora.pt nd nd nd nd nd |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.publisher.none.fl_str_mv |
Journal of Thermal Analysis and Calorimetry |
publisher.none.fl_str_mv |
Journal of Thermal Analysis and Calorimetry |
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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1799136471641227264 |