Adsorption of chia proteins at interfaces: Kinetics of foam and emulsion formation and destabilization
- Autores
- López, Débora Natalia; Boeris, Valeria; Spelzini, Darío; Bonifacino, Carla; Panizzolo, Luis Alberto; Abirached, Cecilia
- Año de publicación
- 2019
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Chia proteins were extracted by solubilisation at pH 10 or 12 and precipitated at pH 4.5. Isolates were named as CPI10 and CPI12, according to their extraction pH, 10 or 12, respectively. The surface properties of both isolates were studied at neutral conditions. Foams were formed by air bubbling and both the formation and destabilization processes were analysed by conductimetry. The extraction pH significantly affected the interfacial properties of chia proteins. The higher surface hydrophobicity in CPI10 led to more flexible proteins with improved foaming properties. Foams formed by CPI10 were more stable than those by CPI12 due to the formation of a thicker interfacial film, which meant a greater ability to retard liquid drainage. Freshly-made coarse emulsions stabilized with CPI12 showed a lower mean droplet size and a significantly lower degree of overall destabilization than those stabilized with CPI10. None of the two emulsions showed flocculating effect.
Fil: López, Débora Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; Argentina. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires". Facultad de Química e Ingeniería-Rosario; Argentina
Fil: Boeris, Valeria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; Argentina. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires". Facultad de Química e Ingeniería-Rosario; Argentina
Fil: Spelzini, Darío. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; Argentina. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires". Facultad de Química e Ingeniería-Rosario; Argentina
Fil: Bonifacino, Carla. Universidad de la República. Facultad de Química; Uruguay
Fil: Panizzolo, Luis Alberto. Universidad de la República. Facultad de Química; Uruguay
Fil: Abirached, Cecilia. Universidad de la República. Facultad de Química; Uruguay - Materia
-
CHIA PROTEIN ISOLATES
INTERFACIAL PROPERTIES - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/114076
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Adsorption of chia proteins at interfaces: Kinetics of foam and emulsion formation and destabilizationLópez, Débora NataliaBoeris, ValeriaSpelzini, DaríoBonifacino, CarlaPanizzolo, Luis AlbertoAbirached, CeciliaCHIA PROTEIN ISOLATESINTERFACIAL PROPERTIEShttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Chia proteins were extracted by solubilisation at pH 10 or 12 and precipitated at pH 4.5. Isolates were named as CPI10 and CPI12, according to their extraction pH, 10 or 12, respectively. The surface properties of both isolates were studied at neutral conditions. Foams were formed by air bubbling and both the formation and destabilization processes were analysed by conductimetry. The extraction pH significantly affected the interfacial properties of chia proteins. The higher surface hydrophobicity in CPI10 led to more flexible proteins with improved foaming properties. Foams formed by CPI10 were more stable than those by CPI12 due to the formation of a thicker interfacial film, which meant a greater ability to retard liquid drainage. Freshly-made coarse emulsions stabilized with CPI12 showed a lower mean droplet size and a significantly lower degree of overall destabilization than those stabilized with CPI10. None of the two emulsions showed flocculating effect.Fil: López, Débora Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; Argentina. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires". Facultad de Química e Ingeniería-Rosario; ArgentinaFil: Boeris, Valeria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; Argentina. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires". Facultad de Química e Ingeniería-Rosario; ArgentinaFil: Spelzini, Darío. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; Argentina. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires". Facultad de Química e Ingeniería-Rosario; ArgentinaFil: Bonifacino, Carla. Universidad de la República. Facultad de Química; UruguayFil: Panizzolo, Luis Alberto. Universidad de la República. Facultad de Química; UruguayFil: Abirached, Cecilia. Universidad de la República. Facultad de Química; UruguayElsevier Science2019-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/114076López, Débora Natalia; Boeris, Valeria; Spelzini, Darío; Bonifacino, Carla; Panizzolo, Luis Alberto; et al.; Adsorption of chia proteins at interfaces: Kinetics of foam and emulsion formation and destabilization; Elsevier Science; Colloids and Surfaces B: Biointerfaces; 180; 5-2019; 503-5070927-7765CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S0927776519302991info:eu-repo/semantics/altIdentifier/doi/10.1016/j.colsurfb.2019.04.067info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:02:44Zoai:ri.conicet.gov.ar:11336/114076instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 10:02:44.817CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Adsorption of chia proteins at interfaces: Kinetics of foam and emulsion formation and destabilization |
title |
Adsorption of chia proteins at interfaces: Kinetics of foam and emulsion formation and destabilization |
spellingShingle |
Adsorption of chia proteins at interfaces: Kinetics of foam and emulsion formation and destabilization López, Débora Natalia CHIA PROTEIN ISOLATES INTERFACIAL PROPERTIES |
title_short |
Adsorption of chia proteins at interfaces: Kinetics of foam and emulsion formation and destabilization |
title_full |
Adsorption of chia proteins at interfaces: Kinetics of foam and emulsion formation and destabilization |
title_fullStr |
Adsorption of chia proteins at interfaces: Kinetics of foam and emulsion formation and destabilization |
title_full_unstemmed |
Adsorption of chia proteins at interfaces: Kinetics of foam and emulsion formation and destabilization |
title_sort |
Adsorption of chia proteins at interfaces: Kinetics of foam and emulsion formation and destabilization |
dc.creator.none.fl_str_mv |
López, Débora Natalia Boeris, Valeria Spelzini, Darío Bonifacino, Carla Panizzolo, Luis Alberto Abirached, Cecilia |
author |
López, Débora Natalia |
author_facet |
López, Débora Natalia Boeris, Valeria Spelzini, Darío Bonifacino, Carla Panizzolo, Luis Alberto Abirached, Cecilia |
author_role |
author |
author2 |
Boeris, Valeria Spelzini, Darío Bonifacino, Carla Panizzolo, Luis Alberto Abirached, Cecilia |
author2_role |
author author author author author |
dc.subject.none.fl_str_mv |
CHIA PROTEIN ISOLATES INTERFACIAL PROPERTIES |
topic |
CHIA PROTEIN ISOLATES INTERFACIAL PROPERTIES |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.4 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Chia proteins were extracted by solubilisation at pH 10 or 12 and precipitated at pH 4.5. Isolates were named as CPI10 and CPI12, according to their extraction pH, 10 or 12, respectively. The surface properties of both isolates were studied at neutral conditions. Foams were formed by air bubbling and both the formation and destabilization processes were analysed by conductimetry. The extraction pH significantly affected the interfacial properties of chia proteins. The higher surface hydrophobicity in CPI10 led to more flexible proteins with improved foaming properties. Foams formed by CPI10 were more stable than those by CPI12 due to the formation of a thicker interfacial film, which meant a greater ability to retard liquid drainage. Freshly-made coarse emulsions stabilized with CPI12 showed a lower mean droplet size and a significantly lower degree of overall destabilization than those stabilized with CPI10. None of the two emulsions showed flocculating effect. Fil: López, Débora Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; Argentina. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires". Facultad de Química e Ingeniería-Rosario; Argentina Fil: Boeris, Valeria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; Argentina. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires". Facultad de Química e Ingeniería-Rosario; Argentina Fil: Spelzini, Darío. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; Argentina. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires". Facultad de Química e Ingeniería-Rosario; Argentina Fil: Bonifacino, Carla. Universidad de la República. Facultad de Química; Uruguay Fil: Panizzolo, Luis Alberto. Universidad de la República. Facultad de Química; Uruguay Fil: Abirached, Cecilia. Universidad de la República. Facultad de Química; Uruguay |
description |
Chia proteins were extracted by solubilisation at pH 10 or 12 and precipitated at pH 4.5. Isolates were named as CPI10 and CPI12, according to their extraction pH, 10 or 12, respectively. The surface properties of both isolates were studied at neutral conditions. Foams were formed by air bubbling and both the formation and destabilization processes were analysed by conductimetry. The extraction pH significantly affected the interfacial properties of chia proteins. The higher surface hydrophobicity in CPI10 led to more flexible proteins with improved foaming properties. Foams formed by CPI10 were more stable than those by CPI12 due to the formation of a thicker interfacial film, which meant a greater ability to retard liquid drainage. Freshly-made coarse emulsions stabilized with CPI12 showed a lower mean droplet size and a significantly lower degree of overall destabilization than those stabilized with CPI10. None of the two emulsions showed flocculating effect. |
publishDate |
2019 |
dc.date.none.fl_str_mv |
2019-05 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
http://hdl.handle.net/11336/114076 López, Débora Natalia; Boeris, Valeria; Spelzini, Darío; Bonifacino, Carla; Panizzolo, Luis Alberto; et al.; Adsorption of chia proteins at interfaces: Kinetics of foam and emulsion formation and destabilization; Elsevier Science; Colloids and Surfaces B: Biointerfaces; 180; 5-2019; 503-507 0927-7765 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/114076 |
identifier_str_mv |
López, Débora Natalia; Boeris, Valeria; Spelzini, Darío; Bonifacino, Carla; Panizzolo, Luis Alberto; et al.; Adsorption of chia proteins at interfaces: Kinetics of foam and emulsion formation and destabilization; Elsevier Science; Colloids and Surfaces B: Biointerfaces; 180; 5-2019; 503-507 0927-7765 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S0927776519302991 info:eu-repo/semantics/altIdentifier/doi/10.1016/j.colsurfb.2019.04.067 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-nd/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Elsevier Science |
publisher.none.fl_str_mv |
Elsevier Science |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
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CONICET Digital (CONICET) |
collection |
CONICET Digital (CONICET) |
instname_str |
Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.name.fl_str_mv |
CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.mail.fl_str_mv |
dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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1842269770967154688 |
score |
13.13397 |