Protein/polysaccharide complexes to stabilize decane-in-water nanoemulsions

Protein/polysaccharide complexes can be formed by electrostatic interactions and may be useful for enhancing the stability of nanoemulsions containing short-chain alkanes, which are highly prone to destabilization by Ostwald ripening. The study aimed to assess the capacity of biopolymer complexes co...

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Autores: Artiga Artigas, María, Reichert, Corina, Salvia Trujillo, Laura, Zeeb, Benjamin, Martín Belloso, Olga, Weiss, Jochen
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2020
País:España
Institución:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repositorio:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:10459.1/69395
Acceso en línea:https://doi.org/10.1007/s11483-019-09622-x
http://hdl.handle.net/10459.1/69395
Access Level:acceso abierto
Palabra clave:Whey protein
Sugar beet pectin
Protein/polysaccharide complexes
Interfacial rheology
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spelling Protein/polysaccharide complexes to stabilize decane-in-water nanoemulsionsArtiga Artigas, MaríaReichert, CorinaSalvia Trujillo, LauraZeeb, BenjaminMartín Belloso, OlgaWeiss, JochenWhey proteinSugar beet pectinProtein/polysaccharide complexesInterfacial rheologyProtein/polysaccharide complexes can be formed by electrostatic interactions and may be useful for enhancing the stability of nanoemulsions containing short-chain alkanes, which are highly prone to destabilization by Ostwald ripening. The study aimed to assess the capacity of biopolymer complexes composed of whey protein isolate (WPI) and sugar beet pectin (SBP) to form and stabilize interfacially structured nanoemulsions. Nanoemulsions were stored for 21 days at room temperature to assess their stability against Ostwald ripening over time. Complexes showed higher emulsifying capacity than biopolymers alone since particle size of complex-stabilized nanoemulsions remained stable (d(4;3)similar to 0.26 mu m) for at least 48 h after preparation, whereas WPI- or SBP-stabilized nanoemulsions were prone to destabilization during the first 24 h reaching values around 1 mu m. Moreover, while the final particle size observed for the latter during the 21 days of storage was around 8 mu m, complex-stabilized nanoemulsions exhibited particle sizes up to 2.34 mu m, which had a direct impact in delaying creaming. Moreover, complex-stabilized nanoemulsions exhibited negative zeta-potential with similar values to those stabilized by SBP (-20.4 and - 22.1 mV, respectively) while the interfacial rheology behavior of complex-stabilized systems was more similar to those stabilized by WPI. This evidences that the protein fraction may be adsorbed at the oil interface thus dominating the interface rheology, whereas pectin chains located on the periphery of the complex and oriented towards the water phase may confer negative interfacial charge to oil droplets. These results indicated that WPI/SBP complexes were more effective than the biopolymers alone in preventing Ostwald ripening in decane-in-water nanoemulsions.This study was funded by the Ministry of Economy, Industry and Competitiveness (MINECO/FEDER, UE) throughout project AGL2015-65975-R. Author María Artiga-Artigas thanks the University of Lleida for their pre-doctoral fellowship. Author Laura Salvia-Trujillo thanks the “Secretaria d’Universitats i Recerca del Departament d’Empresa i Coneixement de la Generalitat de Catalunya” for the Beatriu de Pinós post-doctoral grant BdP2016 00336.Springer Science+Business Media, LLC, part of Springer Nature2020202120202020info:eu-repo/semantics/articleinfo:eu-repo/semantics/acceptedVersionapplication/pdfhttps://doi.org/10.1007/s11483-019-09622-xhttp://hdl.handle.net/10459.1/69395http://hdl.handle.net/10459.1/69395reponame:Recercat. Dipósit de la Recerca de Catalunyainstname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)Inglésinfo:eu-repo/grantAgreement/MINECO//AGL2015-65975-RVersió postprint del document publicat a: https://doi.org/10.1007/s11483-019-09622-xFood Biophysics, 2020, vol. 15, p. 335–345(c) Springer Science+Business Media, LLC, part of Springer Nature, 2020info:eu-repo/semantics/openAccessoai:recercat.cat:10459.1/693952026-05-29T05:05:01Z
dc.title.none.fl_str_mv Protein/polysaccharide complexes to stabilize decane-in-water nanoemulsions
title Protein/polysaccharide complexes to stabilize decane-in-water nanoemulsions
spellingShingle Protein/polysaccharide complexes to stabilize decane-in-water nanoemulsions
Artiga Artigas, María
Whey protein
Sugar beet pectin
Protein/polysaccharide complexes
Interfacial rheology
title_short Protein/polysaccharide complexes to stabilize decane-in-water nanoemulsions
title_full Protein/polysaccharide complexes to stabilize decane-in-water nanoemulsions
title_fullStr Protein/polysaccharide complexes to stabilize decane-in-water nanoemulsions
title_full_unstemmed Protein/polysaccharide complexes to stabilize decane-in-water nanoemulsions
title_sort Protein/polysaccharide complexes to stabilize decane-in-water nanoemulsions
dc.creator.none.fl_str_mv Artiga Artigas, María
Reichert, Corina
Salvia Trujillo, Laura
Zeeb, Benjamin
Martín Belloso, Olga
Weiss, Jochen
author Artiga Artigas, María
author_facet Artiga Artigas, María
Reichert, Corina
Salvia Trujillo, Laura
Zeeb, Benjamin
Martín Belloso, Olga
Weiss, Jochen
author_role author
author2 Reichert, Corina
Salvia Trujillo, Laura
Zeeb, Benjamin
Martín Belloso, Olga
Weiss, Jochen
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Whey protein
Sugar beet pectin
Protein/polysaccharide complexes
Interfacial rheology
topic Whey protein
Sugar beet pectin
Protein/polysaccharide complexes
Interfacial rheology
description Protein/polysaccharide complexes can be formed by electrostatic interactions and may be useful for enhancing the stability of nanoemulsions containing short-chain alkanes, which are highly prone to destabilization by Ostwald ripening. The study aimed to assess the capacity of biopolymer complexes composed of whey protein isolate (WPI) and sugar beet pectin (SBP) to form and stabilize interfacially structured nanoemulsions. Nanoemulsions were stored for 21 days at room temperature to assess their stability against Ostwald ripening over time. Complexes showed higher emulsifying capacity than biopolymers alone since particle size of complex-stabilized nanoemulsions remained stable (d(4;3)similar to 0.26 mu m) for at least 48 h after preparation, whereas WPI- or SBP-stabilized nanoemulsions were prone to destabilization during the first 24 h reaching values around 1 mu m. Moreover, while the final particle size observed for the latter during the 21 days of storage was around 8 mu m, complex-stabilized nanoemulsions exhibited particle sizes up to 2.34 mu m, which had a direct impact in delaying creaming. Moreover, complex-stabilized nanoemulsions exhibited negative zeta-potential with similar values to those stabilized by SBP (-20.4 and - 22.1 mV, respectively) while the interfacial rheology behavior of complex-stabilized systems was more similar to those stabilized by WPI. This evidences that the protein fraction may be adsorbed at the oil interface thus dominating the interface rheology, whereas pectin chains located on the periphery of the complex and oriented towards the water phase may confer negative interfacial charge to oil droplets. These results indicated that WPI/SBP complexes were more effective than the biopolymers alone in preventing Ostwald ripening in decane-in-water nanoemulsions.
publishDate 2020
dc.date.none.fl_str_mv 2020
2020
2020
2021
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv https://doi.org/10.1007/s11483-019-09622-x
http://hdl.handle.net/10459.1/69395
http://hdl.handle.net/10459.1/69395
url https://doi.org/10.1007/s11483-019-09622-x
http://hdl.handle.net/10459.1/69395
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv info:eu-repo/grantAgreement/MINECO//AGL2015-65975-R
Versió postprint del document publicat a: https://doi.org/10.1007/s11483-019-09622-x
Food Biophysics, 2020, vol. 15, p. 335–345
dc.rights.none.fl_str_mv (c) Springer Science+Business Media, LLC, part of Springer Nature, 2020
info:eu-repo/semantics/openAccess
rights_invalid_str_mv (c) Springer Science+Business Media, LLC, part of Springer Nature, 2020
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Springer Science+Business Media, LLC, part of Springer Nature
publisher.none.fl_str_mv Springer Science+Business Media, LLC, part of Springer Nature
dc.source.none.fl_str_mv reponame:Recercat. Dipósit de la Recerca de Catalunya
instname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
instname_str Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
reponame_str Recercat. Dipósit de la Recerca de Catalunya
collection Recercat. Dipósit de la Recerca de Catalunya
repository.name.fl_str_mv
repository.mail.fl_str_mv
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