Electrostatic Interaction between Soy Proteins and Pectin in O/W Emulsions Stabilization by Ultrasound Application

Detalhes bibliográficos
Autor(a) principal: Albano, Kivia M. [UNESP]
Data de Publicação: 2020
Outros Autores: Cavallieri, Ângelo Luiz Fazani, Nicoletti, Vânia R. [UNESP]
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.
id UNSP_2946fa4646efbd77b504cecbb856798d
oai_identifier_str oai:repositorio.unesp.br:11449/199984
network_acronym_str UNSP
network_name_str Repositório Institucional da UNESP
repository_id_str 2946
spelling 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