Morphology of soy protein isolate at oil/water and oil/air interfaces

Detalhes bibliográficos
Autor(a) principal: Fayad,Samira J.
Data de Publicação: 2013
Outros Autores: Zanetti-Ramos,Betina G., Barreto,Pedro L. M., Soldi,Valdir, Minatti,Edson
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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spelling 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
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