Effects of extraction pH of chia protein isolates on functional properties

Autores
López, Débora Natalia; Ingrassia, Romina; Busti, Pablo Andres; Wagner, Jorge Ricardo; Spelzini, Darío; Boeris, Valeria
Año de publicación
2018
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The aim of this work was to study the effect of the extraction pH on the functional properties of chia protein isolates (CPI). Samples were named as CPI10 or CPI12, according to their extraction pH, 10 or 12, respectively. Functional properties were significantly modified by the extraction pH. Color properties revealed that CPI12 presented a lower L* (47.8 ± 0.9 for CPI10 and 30 ± 1 for CPI12). Besides, a higher b* value was obtained for CPI12 (7.0 ± 0.3 for CPI12 and 5.6 ± 0.7 for CPI10), as a result of a higher ash content. CPI12 showed a higher WAC probably due to a higher exposure of polar amino acids (4.4 ± 0.1 g/g and 6.0 ± 0.2 g/g), whereas CPI10 showed a higher ability to bind oil (7.1 ± 0.2 g/g and 6.1 ± 0.2 g/g for CPI10 and CPI12, respectively). CPI10 proved more appropriate as an emulsion stabilizer than CPI12, which could be due to its higher surface hydrophobicity, protein solubility and negative net charge. The d4,3 (μm) was 29.5 ± 0.4 and 20.4 ± 0.3 in emulsions stabilized with CPI12 and CPI10, respectively. Although both isolates underwent heat gelation, they exhibited a weak gel behavior. Overall, CPI10 may be more suitable for the food industry as a meat replacer or extender.
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
Fil: Ingrassia, Romina. 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
Fil: Busti, Pablo Andres. Universidad Nacional de Rosario; Argentina
Fil: Wagner, Jorge Ricardo. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes; Argentina
Fil: Spelzini, Darío. Universidad Nacional de Rosario; Argentina. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires"; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina
Fil: Boeris, Valeria. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires"; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. Universidad Nacional de Rosario; Argentina
Materia
ALKALINE EXTRACTION
EMULSION STABILITY
HEAT GELATION
VEGETABLE PROTEIN
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/100815

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repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Effects of extraction pH of chia protein isolates on functional propertiesLópez, Débora NataliaIngrassia, RominaBusti, Pablo AndresWagner, Jorge RicardoSpelzini, DaríoBoeris, ValeriaALKALINE EXTRACTIONEMULSION STABILITYHEAT GELATIONVEGETABLE PROTEINhttps://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2The aim of this work was to study the effect of the extraction pH on the functional properties of chia protein isolates (CPI). Samples were named as CPI10 or CPI12, according to their extraction pH, 10 or 12, respectively. Functional properties were significantly modified by the extraction pH. Color properties revealed that CPI12 presented a lower L* (47.8 ± 0.9 for CPI10 and 30 ± 1 for CPI12). Besides, a higher b* value was obtained for CPI12 (7.0 ± 0.3 for CPI12 and 5.6 ± 0.7 for CPI10), as a result of a higher ash content. CPI12 showed a higher WAC probably due to a higher exposure of polar amino acids (4.4 ± 0.1 g/g and 6.0 ± 0.2 g/g), whereas CPI10 showed a higher ability to bind oil (7.1 ± 0.2 g/g and 6.1 ± 0.2 g/g for CPI10 and CPI12, respectively). CPI10 proved more appropriate as an emulsion stabilizer than CPI12, which could be due to its higher surface hydrophobicity, protein solubility and negative net charge. The d4,3 (μm) was 29.5 ± 0.4 and 20.4 ± 0.3 in emulsions stabilized with CPI12 and CPI10, respectively. Although both isolates underwent heat gelation, they exhibited a weak gel behavior. Overall, CPI10 may be more suitable for the food industry as a meat replacer or extender.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; ArgentinaFil: Ingrassia, Romina. 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; ArgentinaFil: Busti, Pablo Andres. Universidad Nacional de Rosario; ArgentinaFil: Wagner, Jorge Ricardo. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes; ArgentinaFil: Spelzini, Darío. Universidad Nacional de Rosario; Argentina. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires"; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; ArgentinaFil: Boeris, Valeria. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires"; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. Universidad Nacional de Rosario; ArgentinaElsevier Science2018-11info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/100815López, Débora Natalia; Ingrassia, Romina; Busti, Pablo Andres; Wagner, Jorge Ricardo; Spelzini, Darío; et al.; Effects of extraction pH of chia protein isolates on functional properties; Elsevier Science; LWT - Food Science and Technology; 97; 11-2018; 523-5290023-6438CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0023643818306194info:eu-repo/semantics/altIdentifier/doi/10.1016/j.lwt.2018.07.036info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:46:58Zoai:ri.conicet.gov.ar:11336/100815instacron: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:34982025-09-29 10:46:58.342CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Effects of extraction pH of chia protein isolates on functional properties
title Effects of extraction pH of chia protein isolates on functional properties
spellingShingle Effects of extraction pH of chia protein isolates on functional properties
López, Débora Natalia
ALKALINE EXTRACTION
EMULSION STABILITY
HEAT GELATION
VEGETABLE PROTEIN
title_short Effects of extraction pH of chia protein isolates on functional properties
title_full Effects of extraction pH of chia protein isolates on functional properties
title_fullStr Effects of extraction pH of chia protein isolates on functional properties
title_full_unstemmed Effects of extraction pH of chia protein isolates on functional properties
title_sort Effects of extraction pH of chia protein isolates on functional properties
dc.creator.none.fl_str_mv López, Débora Natalia
Ingrassia, Romina
Busti, Pablo Andres
Wagner, Jorge Ricardo
Spelzini, Darío
Boeris, Valeria
author López, Débora Natalia
author_facet López, Débora Natalia
Ingrassia, Romina
Busti, Pablo Andres
Wagner, Jorge Ricardo
Spelzini, Darío
Boeris, Valeria
author_role author
author2 Ingrassia, Romina
Busti, Pablo Andres
Wagner, Jorge Ricardo
Spelzini, Darío
Boeris, Valeria
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv ALKALINE EXTRACTION
EMULSION STABILITY
HEAT GELATION
VEGETABLE PROTEIN
topic ALKALINE EXTRACTION
EMULSION STABILITY
HEAT GELATION
VEGETABLE PROTEIN
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.11
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv The aim of this work was to study the effect of the extraction pH on the functional properties of chia protein isolates (CPI). Samples were named as CPI10 or CPI12, according to their extraction pH, 10 or 12, respectively. Functional properties were significantly modified by the extraction pH. Color properties revealed that CPI12 presented a lower L* (47.8 ± 0.9 for CPI10 and 30 ± 1 for CPI12). Besides, a higher b* value was obtained for CPI12 (7.0 ± 0.3 for CPI12 and 5.6 ± 0.7 for CPI10), as a result of a higher ash content. CPI12 showed a higher WAC probably due to a higher exposure of polar amino acids (4.4 ± 0.1 g/g and 6.0 ± 0.2 g/g), whereas CPI10 showed a higher ability to bind oil (7.1 ± 0.2 g/g and 6.1 ± 0.2 g/g for CPI10 and CPI12, respectively). CPI10 proved more appropriate as an emulsion stabilizer than CPI12, which could be due to its higher surface hydrophobicity, protein solubility and negative net charge. The d4,3 (μm) was 29.5 ± 0.4 and 20.4 ± 0.3 in emulsions stabilized with CPI12 and CPI10, respectively. Although both isolates underwent heat gelation, they exhibited a weak gel behavior. Overall, CPI10 may be more suitable for the food industry as a meat replacer or extender.
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
Fil: Ingrassia, Romina. 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
Fil: Busti, Pablo Andres. Universidad Nacional de Rosario; Argentina
Fil: Wagner, Jorge Ricardo. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes; Argentina
Fil: Spelzini, Darío. Universidad Nacional de Rosario; Argentina. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires"; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina
Fil: Boeris, Valeria. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires"; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. Universidad Nacional de Rosario; Argentina
description The aim of this work was to study the effect of the extraction pH on the functional properties of chia protein isolates (CPI). Samples were named as CPI10 or CPI12, according to their extraction pH, 10 or 12, respectively. Functional properties were significantly modified by the extraction pH. Color properties revealed that CPI12 presented a lower L* (47.8 ± 0.9 for CPI10 and 30 ± 1 for CPI12). Besides, a higher b* value was obtained for CPI12 (7.0 ± 0.3 for CPI12 and 5.6 ± 0.7 for CPI10), as a result of a higher ash content. CPI12 showed a higher WAC probably due to a higher exposure of polar amino acids (4.4 ± 0.1 g/g and 6.0 ± 0.2 g/g), whereas CPI10 showed a higher ability to bind oil (7.1 ± 0.2 g/g and 6.1 ± 0.2 g/g for CPI10 and CPI12, respectively). CPI10 proved more appropriate as an emulsion stabilizer than CPI12, which could be due to its higher surface hydrophobicity, protein solubility and negative net charge. The d4,3 (μm) was 29.5 ± 0.4 and 20.4 ± 0.3 in emulsions stabilized with CPI12 and CPI10, respectively. Although both isolates underwent heat gelation, they exhibited a weak gel behavior. Overall, CPI10 may be more suitable for the food industry as a meat replacer or extender.
publishDate 2018
dc.date.none.fl_str_mv 2018-11
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/11336/100815
López, Débora Natalia; Ingrassia, Romina; Busti, Pablo Andres; Wagner, Jorge Ricardo; Spelzini, Darío; et al.; Effects of extraction pH of chia protein isolates on functional properties; Elsevier Science; LWT - Food Science and Technology; 97; 11-2018; 523-529
0023-6438
CONICET Digital
CONICET
url http://hdl.handle.net/11336/100815
identifier_str_mv López, Débora Natalia; Ingrassia, Romina; Busti, Pablo Andres; Wagner, Jorge Ricardo; Spelzini, Darío; et al.; Effects of extraction pH of chia protein isolates on functional properties; Elsevier Science; LWT - Food Science and Technology; 97; 11-2018; 523-529
0023-6438
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/pii/S0023643818306194
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.lwt.2018.07.036
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
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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)
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reponame_str CONICET Digital (CONICET)
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repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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