Morphology of soy protein isolate at oil/water and oil/air interfaces
Autor(a) principal: | |
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Data de Publicação: | 2013 |
Outros Autores: | , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Journal of the Brazilian Chemical Society (Online) |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532013000600016 |
Resumo: | Herein, the emulsifying properties of soy protein isolate (SPI) were highlighted by showing that the macromolecules undergo conformational changes when adsorbed at interfaces. The conformation of protein chains nested at the interfacial region of oil in water (o/w) emulsions by means of X-ray scattering (SAXS) and direct imaging (scanning electron microscopy (SEM)) techniques was investigated. The mean radius of gyration (Rg) for SPI (aq) is 20 nm and increases up to 30 nm in o/w emulsions; the proteins act as amphiphilic molecules by exposing their hydrophobic core to the oil and their hydrophilic amino acid residues to the water phase. By spray drying the emulsions, it was also possible to measure the size (Rg = 40 nm) and to evaluate the morphology of these proteins at the oil/air interface of the respective microcapsules. The walls of microcapsules are fractals of clustered objects with rough surfaces, which are smoothed by the presence of a cross-linking agent. |
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Morphology of soy protein isolate at oil/water and oil/air interfacesinterfaceemulsionproteinsurfacemicrocapsulesHerein, the emulsifying properties of soy protein isolate (SPI) were highlighted by showing that the macromolecules undergo conformational changes when adsorbed at interfaces. The conformation of protein chains nested at the interfacial region of oil in water (o/w) emulsions by means of X-ray scattering (SAXS) and direct imaging (scanning electron microscopy (SEM)) techniques was investigated. The mean radius of gyration (Rg) for SPI (aq) is 20 nm and increases up to 30 nm in o/w emulsions; the proteins act as amphiphilic molecules by exposing their hydrophobic core to the oil and their hydrophilic amino acid residues to the water phase. By spray drying the emulsions, it was also possible to measure the size (Rg = 40 nm) and to evaluate the morphology of these proteins at the oil/air interface of the respective microcapsules. The walls of microcapsules are fractals of clustered objects with rough surfaces, which are smoothed by the presence of a cross-linking agent.Sociedade Brasileira de Química2013-06-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532013000600016Journal of the Brazilian Chemical Society v.24 n.6 2013reponame:Journal of the Brazilian Chemical Society (Online)instname:Sociedade Brasileira de Química (SBQ)instacron:SBQ10.5935/0103-5053.20130130info:eu-repo/semantics/openAccessFayad,Samira J.Zanetti-Ramos,Betina G.Barreto,Pedro L. M.Soldi,ValdirMinatti,Edsoneng2013-06-27T00:00:00Zoai:scielo:S0103-50532013000600016Revistahttp://jbcs.sbq.org.brONGhttps://old.scielo.br/oai/scielo-oai.php||office@jbcs.sbq.org.br1678-47900103-5053opendoar:2013-06-27T00:00Journal of the Brazilian Chemical Society (Online) - Sociedade Brasileira de Química (SBQ)false |
dc.title.none.fl_str_mv |
Morphology of soy protein isolate at oil/water and oil/air interfaces |
title |
Morphology of soy protein isolate at oil/water and oil/air interfaces |
spellingShingle |
Morphology of soy protein isolate at oil/water and oil/air interfaces Fayad,Samira J. interface emulsion protein surface microcapsules |
title_short |
Morphology of soy protein isolate at oil/water and oil/air interfaces |
title_full |
Morphology of soy protein isolate at oil/water and oil/air interfaces |
title_fullStr |
Morphology of soy protein isolate at oil/water and oil/air interfaces |
title_full_unstemmed |
Morphology of soy protein isolate at oil/water and oil/air interfaces |
title_sort |
Morphology of soy protein isolate at oil/water and oil/air interfaces |
author |
Fayad,Samira J. |
author_facet |
Fayad,Samira J. Zanetti-Ramos,Betina G. Barreto,Pedro L. M. Soldi,Valdir Minatti,Edson |
author_role |
author |
author2 |
Zanetti-Ramos,Betina G. Barreto,Pedro L. M. Soldi,Valdir Minatti,Edson |
author2_role |
author author author author |
dc.contributor.author.fl_str_mv |
Fayad,Samira J. Zanetti-Ramos,Betina G. Barreto,Pedro L. M. Soldi,Valdir Minatti,Edson |
dc.subject.por.fl_str_mv |
interface emulsion protein surface microcapsules |
topic |
interface emulsion protein surface microcapsules |
description |
Herein, the emulsifying properties of soy protein isolate (SPI) were highlighted by showing that the macromolecules undergo conformational changes when adsorbed at interfaces. The conformation of protein chains nested at the interfacial region of oil in water (o/w) emulsions by means of X-ray scattering (SAXS) and direct imaging (scanning electron microscopy (SEM)) techniques was investigated. The mean radius of gyration (Rg) for SPI (aq) is 20 nm and increases up to 30 nm in o/w emulsions; the proteins act as amphiphilic molecules by exposing their hydrophobic core to the oil and their hydrophilic amino acid residues to the water phase. By spray drying the emulsions, it was also possible to measure the size (Rg = 40 nm) and to evaluate the morphology of these proteins at the oil/air interface of the respective microcapsules. The walls of microcapsules are fractals of clustered objects with rough surfaces, which are smoothed by the presence of a cross-linking agent. |
publishDate |
2013 |
dc.date.none.fl_str_mv |
2013-06-01 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532013000600016 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532013000600016 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.5935/0103-5053.20130130 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
text/html |
dc.publisher.none.fl_str_mv |
Sociedade Brasileira de Química |
publisher.none.fl_str_mv |
Sociedade Brasileira de Química |
dc.source.none.fl_str_mv |
Journal of the Brazilian Chemical Society v.24 n.6 2013 reponame:Journal of the Brazilian Chemical Society (Online) instname:Sociedade Brasileira de Química (SBQ) instacron:SBQ |
instname_str |
Sociedade Brasileira de Química (SBQ) |
instacron_str |
SBQ |
institution |
SBQ |
reponame_str |
Journal of the Brazilian Chemical Society (Online) |
collection |
Journal of the Brazilian Chemical Society (Online) |
repository.name.fl_str_mv |
Journal of the Brazilian Chemical Society (Online) - Sociedade Brasileira de Química (SBQ) |
repository.mail.fl_str_mv |
||office@jbcs.sbq.org.br |
_version_ |
1750318174899798016 |