Isoflavone aglycone content and the thermal, functional, and structural properties of soy protein isolates prepared from hydrothermally treated soybeans.
Autor(a) principal: | |
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Data de Publicação: | 2014 |
Outros Autores: | , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice) |
Texto Completo: | http://www.alice.cnptia.embrapa.br/alice/handle/doc/1041964 |
Resumo: | Soybeans were hydrothermally treated at 2 different temperatures (40 °C and 60 °C) and for 4 different hydration times (4, 8, 12, and 16 h) to (i) increase the isoflavone aglycone content in a soy protein isolate and (ii) evaluate the changes in thermal, functional, and structural properties of a soy protein isolate as a function of hydrothermal treatment conditions. Our study is the first to evaluate aglycone content, extraction yield, ?-glucosidase activity, differential scanning calorimetry, protein digestibility, scanning electron microscopy, water absorption capacity (WAC), foaming capacity (FC), and foaming stability of soy protein isolates prepared from hydrothermally treated soybeans. For aglycone enhancement and the extraction yield maintenance of soy protein isolates, the condition of 40 °C for 12 h was the best soybean hydrothermal treatment. The structural rearrangement of proteins that occurred with the hydrothermal treatment most likely promoted the capacity of proteins to bind to aglycone. Moreover, the structure shape and size of soy protein isolates verified by scanning electron microscopy appears to be related to the formation of hydrophobic surfaces and hydrophobic zones at 40 °C and 60 °C, respectively, affecting the protein digestibility, WAC, and FC of soy protein isolates. |
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Isoflavone aglycone content and the thermal, functional, and structural properties of soy protein isolates prepared from hydrothermally treated soybeans.SojaSoybeans were hydrothermally treated at 2 different temperatures (40 °C and 60 °C) and for 4 different hydration times (4, 8, 12, and 16 h) to (i) increase the isoflavone aglycone content in a soy protein isolate and (ii) evaluate the changes in thermal, functional, and structural properties of a soy protein isolate as a function of hydrothermal treatment conditions. Our study is the first to evaluate aglycone content, extraction yield, ?-glucosidase activity, differential scanning calorimetry, protein digestibility, scanning electron microscopy, water absorption capacity (WAC), foaming capacity (FC), and foaming stability of soy protein isolates prepared from hydrothermally treated soybeans. For aglycone enhancement and the extraction yield maintenance of soy protein isolates, the condition of 40 °C for 12 h was the best soybean hydrothermal treatment. The structural rearrangement of proteins that occurred with the hydrothermal treatment most likely promoted the capacity of proteins to bind to aglycone. Moreover, the structure shape and size of soy protein isolates verified by scanning electron microscopy appears to be related to the formation of hydrophobic surfaces and hydrophobic zones at 40 °C and 60 °C, respectively, affecting the protein digestibility, WAC, and FC of soy protein isolates.Ana Paula Wally-Vallim, UFPEL; Nathan Levien Vanier, UFPEL; Elessandra da Rosa Zavareze, UFPEL; Rui Carlos Zambiazi, UFPEL; LUIS ANTONIO SUITA DE CASTRO, CPACT; Manoel Artigas Schirmer, UFPEL; Moacir Cardoso Elias, UFPEL.WALLY-VALIM, A, P.VANIER, N. L.ZAVAREZE, E. DA R.ZAMBIAZI, R. C.CASTRO, L. A. S. deSCHIRMER, M. A.ELIAS, M. C.2016-03-30T05:46:20Z2016-03-30T05:46:20Z2016-03-2920142016-03-30T05:46:20Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleJournal of Food Science, v. 79, n. 7, p. E1351-E1358, 2014.1750-3841http://www.alice.cnptia.embrapa.br/alice/handle/doc/1041964enginfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice)instname:Empresa Brasileira de Pesquisa Agropecuária (Embrapa)instacron:EMBRAPA2017-08-16T03:07:41Zoai:www.alice.cnptia.embrapa.br:doc/1041964Repositório InstitucionalPUBhttps://www.alice.cnptia.embrapa.br/oai/requestopendoar:21542017-08-16T03:07:41falseRepositório InstitucionalPUBhttps://www.alice.cnptia.embrapa.br/oai/requestcg-riaa@embrapa.bropendoar:21542017-08-16T03:07:41Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice) - Empresa Brasileira de Pesquisa Agropecuária (Embrapa)false |
dc.title.none.fl_str_mv |
Isoflavone aglycone content and the thermal, functional, and structural properties of soy protein isolates prepared from hydrothermally treated soybeans. |
title |
Isoflavone aglycone content and the thermal, functional, and structural properties of soy protein isolates prepared from hydrothermally treated soybeans. |
spellingShingle |
Isoflavone aglycone content and the thermal, functional, and structural properties of soy protein isolates prepared from hydrothermally treated soybeans. WALLY-VALIM, A, P. Soja |
title_short |
Isoflavone aglycone content and the thermal, functional, and structural properties of soy protein isolates prepared from hydrothermally treated soybeans. |
title_full |
Isoflavone aglycone content and the thermal, functional, and structural properties of soy protein isolates prepared from hydrothermally treated soybeans. |
title_fullStr |
Isoflavone aglycone content and the thermal, functional, and structural properties of soy protein isolates prepared from hydrothermally treated soybeans. |
title_full_unstemmed |
Isoflavone aglycone content and the thermal, functional, and structural properties of soy protein isolates prepared from hydrothermally treated soybeans. |
title_sort |
Isoflavone aglycone content and the thermal, functional, and structural properties of soy protein isolates prepared from hydrothermally treated soybeans. |
author |
WALLY-VALIM, A, P. |
author_facet |
WALLY-VALIM, A, P. VANIER, N. L. ZAVAREZE, E. DA R. ZAMBIAZI, R. C. CASTRO, L. A. S. de SCHIRMER, M. A. ELIAS, M. C. |
author_role |
author |
author2 |
VANIER, N. L. ZAVAREZE, E. DA R. ZAMBIAZI, R. C. CASTRO, L. A. S. de SCHIRMER, M. A. ELIAS, M. C. |
author2_role |
author author author author author author |
dc.contributor.none.fl_str_mv |
Ana Paula Wally-Vallim, UFPEL; Nathan Levien Vanier, UFPEL; Elessandra da Rosa Zavareze, UFPEL; Rui Carlos Zambiazi, UFPEL; LUIS ANTONIO SUITA DE CASTRO, CPACT; Manoel Artigas Schirmer, UFPEL; Moacir Cardoso Elias, UFPEL. |
dc.contributor.author.fl_str_mv |
WALLY-VALIM, A, P. VANIER, N. L. ZAVAREZE, E. DA R. ZAMBIAZI, R. C. CASTRO, L. A. S. de SCHIRMER, M. A. ELIAS, M. C. |
dc.subject.por.fl_str_mv |
Soja |
topic |
Soja |
description |
Soybeans were hydrothermally treated at 2 different temperatures (40 °C and 60 °C) and for 4 different hydration times (4, 8, 12, and 16 h) to (i) increase the isoflavone aglycone content in a soy protein isolate and (ii) evaluate the changes in thermal, functional, and structural properties of a soy protein isolate as a function of hydrothermal treatment conditions. Our study is the first to evaluate aglycone content, extraction yield, ?-glucosidase activity, differential scanning calorimetry, protein digestibility, scanning electron microscopy, water absorption capacity (WAC), foaming capacity (FC), and foaming stability of soy protein isolates prepared from hydrothermally treated soybeans. For aglycone enhancement and the extraction yield maintenance of soy protein isolates, the condition of 40 °C for 12 h was the best soybean hydrothermal treatment. The structural rearrangement of proteins that occurred with the hydrothermal treatment most likely promoted the capacity of proteins to bind to aglycone. Moreover, the structure shape and size of soy protein isolates verified by scanning electron microscopy appears to be related to the formation of hydrophobic surfaces and hydrophobic zones at 40 °C and 60 °C, respectively, affecting the protein digestibility, WAC, and FC of soy protein isolates. |
publishDate |
2014 |
dc.date.none.fl_str_mv |
2014 2016-03-30T05:46:20Z 2016-03-30T05:46:20Z 2016-03-29 2016-03-30T05:46:20Z |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/publishedVersion info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
Journal of Food Science, v. 79, n. 7, p. E1351-E1358, 2014. 1750-3841 http://www.alice.cnptia.embrapa.br/alice/handle/doc/1041964 |
identifier_str_mv |
Journal of Food Science, v. 79, n. 7, p. E1351-E1358, 2014. 1750-3841 |
url |
http://www.alice.cnptia.embrapa.br/alice/handle/doc/1041964 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.source.none.fl_str_mv |
reponame:Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice) instname:Empresa Brasileira de Pesquisa Agropecuária (Embrapa) instacron:EMBRAPA |
instname_str |
Empresa Brasileira de Pesquisa Agropecuária (Embrapa) |
instacron_str |
EMBRAPA |
institution |
EMBRAPA |
reponame_str |
Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice) |
collection |
Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice) |
repository.name.fl_str_mv |
Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice) - Empresa Brasileira de Pesquisa Agropecuária (Embrapa) |
repository.mail.fl_str_mv |
cg-riaa@embrapa.br |
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1794503420172828672 |