Electrostatic Interaction between Soy Proteins and Pectin in O/W Emulsions Stabilization by Ultrasound Application
Autor(a) principal: | |
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Data de Publicação: | 2020 |
Outros Autores: | , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1007/s11483-020-09625-z http://hdl.handle.net/11449/199984 |
Resumo: | Proteins and polysaccharides can play the part of emulsifiers and stabilizers, yet emulsions stabilization may be improved through a protein:polysaccharide complexation based on electrostatic interactions. The chosen homogenization method and the protein:polysaccharide ratio at an adequate pH may affect complexation and its ability as an emulsion stabilizer. We evaluate the effects of ultrasound homogenization and soy protein isolate (SPI) and high methoxyl pectin (PEC) ratio to generate protein:polysaccharide complexes by electrostatic interactions. Moreover, emulsions stabilized by SPI:PEC complexes with 5, 10, 15 % soybean oil contents were evaluated after sonication to assess emulsions stability improvements. SPI and PEC showed strong interaction at pH 3.5, with higher complexation at higher protein ratio (4:1). Sonication reduced complex particle size, creating homogeneous and shear-thinning systems. SPI:PEC 1:1 emulsions had Newtonian behavior, smaller droplets, and remained stable for seven days. At SPI:PEC ratio of 4:1 emulsions had shear-thinning behavior, yet larger droplets and high creaming indexes, thus indicating destabilization by gravitational separation with cream phase and showing droplets with bimodal distribution (1.3-200 μm). Through heating-cooling ramps, temperature effect on rheological behavior of emulsions and pure biopolymers was assessed. 4:1 emulsions showed rheological behavior with a predominant effect of SPI, whereas 1:1 emulsions predominantly showed pectin characteristics. Emulsion stability was greatly affected by SPI:PEC ratio, since the pectin proportion had a strong influence on the emulsions behavior. Moreover, sonication was a fundamental parameter to increase SPI:PEC complexes effectiveness as emulsion stabilizers and use these systems to formulate foods with low oil contents. |
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Electrostatic Interaction between Soy Proteins and Pectin in O/W Emulsions Stabilization by Ultrasound ApplicationComplex CoacervationDroplet size distributionEmulsion stabilityHigh Methoxyl pectinRheologySonicationProteins and polysaccharides can play the part of emulsifiers and stabilizers, yet emulsions stabilization may be improved through a protein:polysaccharide complexation based on electrostatic interactions. The chosen homogenization method and the protein:polysaccharide ratio at an adequate pH may affect complexation and its ability as an emulsion stabilizer. We evaluate the effects of ultrasound homogenization and soy protein isolate (SPI) and high methoxyl pectin (PEC) ratio to generate protein:polysaccharide complexes by electrostatic interactions. Moreover, emulsions stabilized by SPI:PEC complexes with 5, 10, 15 % soybean oil contents were evaluated after sonication to assess emulsions stability improvements. SPI and PEC showed strong interaction at pH 3.5, with higher complexation at higher protein ratio (4:1). Sonication reduced complex particle size, creating homogeneous and shear-thinning systems. SPI:PEC 1:1 emulsions had Newtonian behavior, smaller droplets, and remained stable for seven days. At SPI:PEC ratio of 4:1 emulsions had shear-thinning behavior, yet larger droplets and high creaming indexes, thus indicating destabilization by gravitational separation with cream phase and showing droplets with bimodal distribution (1.3-200 μm). Through heating-cooling ramps, temperature effect on rheological behavior of emulsions and pure biopolymers was assessed. 4:1 emulsions showed rheological behavior with a predominant effect of SPI, whereas 1:1 emulsions predominantly showed pectin characteristics. Emulsion stability was greatly affected by SPI:PEC ratio, since the pectin proportion had a strong influence on the emulsions behavior. Moreover, sonication was a fundamental parameter to increase SPI:PEC complexes effectiveness as emulsion stabilizers and use these systems to formulate foods with low oil contents.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Department of Food Engineering and Technology São Paulo State University (UNESP) Institute of Biosciences Humanities and Exact Sciences (Ibilce) - Campus São José do Rio Preto, Cristóvão Colombo St., 2265Center of Nature Sciences (Lagoa do Sino) Federal University of São Carlos (UFSCar), Campus Buri, Highway Lauri Simões de Barros, Km 12- SP-189Department of Food Engineering and Technology São Paulo State University (UNESP) Institute of Biosciences Humanities and Exact Sciences (Ibilce) - Campus São José do Rio Preto, Cristóvão Colombo St., 2265FAPESP: 2013/10842-9FAPESP: 2014/02910-7Universidade Estadual Paulista (Unesp)Universidade Federal de São Carlos (UFSCar)Albano, Kivia M. [UNESP]Cavallieri, Ângelo Luiz FazaniNicoletti, Vânia R. [UNESP]2020-12-12T01:54:33Z2020-12-12T01:54:33Z2020-09-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article297-312http://dx.doi.org/10.1007/s11483-020-09625-zFood Biophysics, v. 15, n. 3, p. 297-312, 2020.1557-18661557-1858http://hdl.handle.net/11449/19998410.1007/s11483-020-09625-z2-s2.0-85078307972Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengFood Biophysicsinfo:eu-repo/semantics/openAccess2021-10-23T10:18:35Zoai:repositorio.unesp.br:11449/199984Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T17:00:31.839967Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Electrostatic Interaction between Soy Proteins and Pectin in O/W Emulsions Stabilization by Ultrasound Application |
title |
Electrostatic Interaction between Soy Proteins and Pectin in O/W Emulsions Stabilization by Ultrasound Application |
spellingShingle |
Electrostatic Interaction between Soy Proteins and Pectin in O/W Emulsions Stabilization by Ultrasound Application Albano, Kivia M. [UNESP] Complex Coacervation Droplet size distribution Emulsion stability High Methoxyl pectin Rheology Sonication |
title_short |
Electrostatic Interaction between Soy Proteins and Pectin in O/W Emulsions Stabilization by Ultrasound Application |
title_full |
Electrostatic Interaction between Soy Proteins and Pectin in O/W Emulsions Stabilization by Ultrasound Application |
title_fullStr |
Electrostatic Interaction between Soy Proteins and Pectin in O/W Emulsions Stabilization by Ultrasound Application |
title_full_unstemmed |
Electrostatic Interaction between Soy Proteins and Pectin in O/W Emulsions Stabilization by Ultrasound Application |
title_sort |
Electrostatic Interaction between Soy Proteins and Pectin in O/W Emulsions Stabilization by Ultrasound Application |
author |
Albano, Kivia M. [UNESP] |
author_facet |
Albano, Kivia M. [UNESP] Cavallieri, Ângelo Luiz Fazani Nicoletti, Vânia R. [UNESP] |
author_role |
author |
author2 |
Cavallieri, Ângelo Luiz Fazani Nicoletti, Vânia R. [UNESP] |
author2_role |
author author |
dc.contributor.none.fl_str_mv |
Universidade Estadual Paulista (Unesp) Universidade Federal de São Carlos (UFSCar) |
dc.contributor.author.fl_str_mv |
Albano, Kivia M. [UNESP] Cavallieri, Ângelo Luiz Fazani Nicoletti, Vânia R. [UNESP] |
dc.subject.por.fl_str_mv |
Complex Coacervation Droplet size distribution Emulsion stability High Methoxyl pectin Rheology Sonication |
topic |
Complex Coacervation Droplet size distribution Emulsion stability High Methoxyl pectin Rheology Sonication |
description |
Proteins and polysaccharides can play the part of emulsifiers and stabilizers, yet emulsions stabilization may be improved through a protein:polysaccharide complexation based on electrostatic interactions. The chosen homogenization method and the protein:polysaccharide ratio at an adequate pH may affect complexation and its ability as an emulsion stabilizer. We evaluate the effects of ultrasound homogenization and soy protein isolate (SPI) and high methoxyl pectin (PEC) ratio to generate protein:polysaccharide complexes by electrostatic interactions. Moreover, emulsions stabilized by SPI:PEC complexes with 5, 10, 15 % soybean oil contents were evaluated after sonication to assess emulsions stability improvements. SPI and PEC showed strong interaction at pH 3.5, with higher complexation at higher protein ratio (4:1). Sonication reduced complex particle size, creating homogeneous and shear-thinning systems. SPI:PEC 1:1 emulsions had Newtonian behavior, smaller droplets, and remained stable for seven days. At SPI:PEC ratio of 4:1 emulsions had shear-thinning behavior, yet larger droplets and high creaming indexes, thus indicating destabilization by gravitational separation with cream phase and showing droplets with bimodal distribution (1.3-200 μm). Through heating-cooling ramps, temperature effect on rheological behavior of emulsions and pure biopolymers was assessed. 4:1 emulsions showed rheological behavior with a predominant effect of SPI, whereas 1:1 emulsions predominantly showed pectin characteristics. Emulsion stability was greatly affected by SPI:PEC ratio, since the pectin proportion had a strong influence on the emulsions behavior. Moreover, sonication was a fundamental parameter to increase SPI:PEC complexes effectiveness as emulsion stabilizers and use these systems to formulate foods with low oil contents. |
publishDate |
2020 |
dc.date.none.fl_str_mv |
2020-12-12T01:54:33Z 2020-12-12T01:54:33Z 2020-09-01 |
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://dx.doi.org/10.1007/s11483-020-09625-z Food Biophysics, v. 15, n. 3, p. 297-312, 2020. 1557-1866 1557-1858 http://hdl.handle.net/11449/199984 10.1007/s11483-020-09625-z 2-s2.0-85078307972 |
url |
http://dx.doi.org/10.1007/s11483-020-09625-z http://hdl.handle.net/11449/199984 |
identifier_str_mv |
Food Biophysics, v. 15, n. 3, p. 297-312, 2020. 1557-1866 1557-1858 10.1007/s11483-020-09625-z 2-s2.0-85078307972 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Food Biophysics |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
297-312 |
dc.source.none.fl_str_mv |
Scopus reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
_version_ |
1808128738611691520 |