“Structural characterization of protein isolates obtained from chia (Salvia hispanica L.) seeds”

Autores
López, Débora Natalia; Ingrassia, Romina; Busti, Pablo Andres; Bonino, Julia; Delgado, Juan Francisco; Wagner, Jorge Ricardo; Boeris, Valeria; Spelzini, Darío
Año de publicación
2018
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Chia protein isolates (CPI) were obtained through isoelectric precipitation under two different conditions in order to compare their structural properties. Extraction was carried out at pH 10 or 12, whereas precipitation pH was fixed at 4.5. Samples were named as CPI10 or CPI12, according to their extraction pH (10 or 12, respectively). The recovery of chia proteins was higher when the extraction was carried out at pH 12 (17% for CPI12 and 13% for CPI10); however, CPI12 protein content (775 g/kg) was slightly lower than CPI10 protein content (782 g/kg). Both samples showed similar SDS-PAGE pattern. Protein dispersions of both isolates led to highly stabilized particles due to their negative ζ potential (around −54 mV). CPI10 has a higher proportion of small particles in suspension, revealed by a lower d3,2 value. Spectroscopic techniques showed that CPI10 presented higher content of β-helix than CPI12, resulting in higher thermal stability. This observation was supported by FT-IR spectroscopy since CPI10 presented less unordered structure than CPI12. The energy of endotherms obtained in CPI12 was considerably lower than in CPI10. Extraction at higher alkaline conditions led to a more denatured protein conformation with a higher content of random structure (18.1% for CPI10 and 22.9% for CPI12).
Fil: López, Débora Natalia. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnol.conicet - Rosario. Unidad de Direccion; Argentina
Fil: Ingrassia, Romina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnol.conicet - Rosario. Unidad de Direccion; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina
Fil: Busti, Pablo Andres. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina
Fil: Bonino, Julia. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires"; Argentina
Fil: Delgado, Juan Francisco. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnol.conicet - Rosario. Unidad de Direccion; Argentina. Universidad Nacional de Quilmes; Argentina
Fil: Wagner, Jorge Ricardo. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Boeris, Valeria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnol.conicet - Rosario. Unidad de Direccion; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina
Fil: Spelzini, Darío. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnol.conicet - Rosario. Unidad de Direccion; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina
Materia
ALKALINE EXTRACTION
SPECTROSCOPIC CHARACTERIZATION
THERMAL STABILITY
VEGETABLE PROTEIN
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/93502
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/93502
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling “Structural characterization of protein isolates obtained from chia (Salvia hispanica L.) seeds”López, Débora NataliaIngrassia, RominaBusti, Pablo AndresBonino, JuliaDelgado, Juan FranciscoWagner, Jorge RicardoBoeris, ValeriaSpelzini, DaríoALKALINE EXTRACTIONSPECTROSCOPIC CHARACTERIZATIONTHERMAL STABILITYVEGETABLE PROTEINhttps://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2Chia protein isolates (CPI) were obtained through isoelectric precipitation under two different conditions in order to compare their structural properties. Extraction was carried out at pH 10 or 12, whereas precipitation pH was fixed at 4.5. Samples were named as CPI10 or CPI12, according to their extraction pH (10 or 12, respectively). The recovery of chia proteins was higher when the extraction was carried out at pH 12 (17% for CPI12 and 13% for CPI10); however, CPI12 protein content (775 g/kg) was slightly lower than CPI10 protein content (782 g/kg). Both samples showed similar SDS-PAGE pattern. Protein dispersions of both isolates led to highly stabilized particles due to their negative ζ potential (around −54 mV). CPI10 has a higher proportion of small particles in suspension, revealed by a lower d3,2 value. Spectroscopic techniques showed that CPI10 presented higher content of β-helix than CPI12, resulting in higher thermal stability. This observation was supported by FT-IR spectroscopy since CPI10 presented less unordered structure than CPI12. The energy of endotherms obtained in CPI12 was considerably lower than in CPI10. Extraction at higher alkaline conditions led to a more denatured protein conformation with a higher content of random structure (18.1% for CPI10 and 22.9% for CPI12).Fil: López, Débora Natalia. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnol.conicet - Rosario. Unidad de Direccion; ArgentinaFil: Ingrassia, Romina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnol.conicet - Rosario. Unidad de Direccion; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; ArgentinaFil: Busti, Pablo Andres. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; ArgentinaFil: Bonino, Julia. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires"; ArgentinaFil: Delgado, Juan Francisco. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnol.conicet - Rosario. Unidad de Direccion; Argentina. Universidad Nacional de Quilmes; ArgentinaFil: Wagner, Jorge Ricardo. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Boeris, Valeria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnol.conicet - Rosario. Unidad de Direccion; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; ArgentinaFil: Spelzini, Darío. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnol.conicet - Rosario. Unidad de Direccion; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; ArgentinaElsevier Science2018-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/93502López, Débora Natalia; Ingrassia, Romina; Busti, Pablo Andres; Bonino, Julia; Delgado, Juan Francisco; et al.; “Structural characterization of protein isolates obtained from chia (Salvia hispanica L.) seeds”; Elsevier Science; LWT - Food Science and Technology; 90; 4-2018; 396-4020023-6438CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.lwt.2017.12.060info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0023643817309544info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T14:28:44Zoai:ri.conicet.gov.ar:11336/93502instacron: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:34982025-10-15 14:28:44.863CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv “Structural characterization of protein isolates obtained from chia (Salvia hispanica L.) seeds”
title “Structural characterization of protein isolates obtained from chia (Salvia hispanica L.) seeds”
spellingShingle “Structural characterization of protein isolates obtained from chia (Salvia hispanica L.) seeds”
López, Débora Natalia
ALKALINE EXTRACTION
SPECTROSCOPIC CHARACTERIZATION
THERMAL STABILITY
VEGETABLE PROTEIN
title_short “Structural characterization of protein isolates obtained from chia (Salvia hispanica L.) seeds”
title_full “Structural characterization of protein isolates obtained from chia (Salvia hispanica L.) seeds”
title_fullStr “Structural characterization of protein isolates obtained from chia (Salvia hispanica L.) seeds”
title_full_unstemmed “Structural characterization of protein isolates obtained from chia (Salvia hispanica L.) seeds”
title_sort “Structural characterization of protein isolates obtained from chia (Salvia hispanica L.) seeds”
dc.creator.none.fl_str_mv López, Débora Natalia
Ingrassia, Romina
Busti, Pablo Andres
Bonino, Julia
Delgado, Juan Francisco
Wagner, Jorge Ricardo
Boeris, Valeria
Spelzini, Darío
author López, Débora Natalia
author_facet López, Débora Natalia
Ingrassia, Romina
Busti, Pablo Andres
Bonino, Julia
Delgado, Juan Francisco
Wagner, Jorge Ricardo
Boeris, Valeria
Spelzini, Darío
author_role author
author2 Ingrassia, Romina
Busti, Pablo Andres
Bonino, Julia
Delgado, Juan Francisco
Wagner, Jorge Ricardo
Boeris, Valeria
Spelzini, Darío
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv ALKALINE EXTRACTION
SPECTROSCOPIC CHARACTERIZATION
THERMAL STABILITY
VEGETABLE PROTEIN
topic ALKALINE EXTRACTION
SPECTROSCOPIC CHARACTERIZATION
THERMAL STABILITY
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 Chia protein isolates (CPI) were obtained through isoelectric precipitation under two different conditions in order to compare their structural properties. Extraction was carried out at pH 10 or 12, whereas precipitation pH was fixed at 4.5. Samples were named as CPI10 or CPI12, according to their extraction pH (10 or 12, respectively). The recovery of chia proteins was higher when the extraction was carried out at pH 12 (17% for CPI12 and 13% for CPI10); however, CPI12 protein content (775 g/kg) was slightly lower than CPI10 protein content (782 g/kg). Both samples showed similar SDS-PAGE pattern. Protein dispersions of both isolates led to highly stabilized particles due to their negative ζ potential (around −54 mV). CPI10 has a higher proportion of small particles in suspension, revealed by a lower d3,2 value. Spectroscopic techniques showed that CPI10 presented higher content of β-helix than CPI12, resulting in higher thermal stability. This observation was supported by FT-IR spectroscopy since CPI10 presented less unordered structure than CPI12. The energy of endotherms obtained in CPI12 was considerably lower than in CPI10. Extraction at higher alkaline conditions led to a more denatured protein conformation with a higher content of random structure (18.1% for CPI10 and 22.9% for CPI12).
Fil: López, Débora Natalia. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnol.conicet - Rosario. Unidad de Direccion; Argentina
Fil: Ingrassia, Romina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnol.conicet - Rosario. Unidad de Direccion; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina
Fil: Busti, Pablo Andres. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina
Fil: Bonino, Julia. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires"; Argentina
Fil: Delgado, Juan Francisco. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnol.conicet - Rosario. Unidad de Direccion; Argentina. Universidad Nacional de Quilmes; Argentina
Fil: Wagner, Jorge Ricardo. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Boeris, Valeria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnol.conicet - Rosario. Unidad de Direccion; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina
Fil: Spelzini, Darío. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnol.conicet - Rosario. Unidad de Direccion; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina
description Chia protein isolates (CPI) were obtained through isoelectric precipitation under two different conditions in order to compare their structural properties. Extraction was carried out at pH 10 or 12, whereas precipitation pH was fixed at 4.5. Samples were named as CPI10 or CPI12, according to their extraction pH (10 or 12, respectively). The recovery of chia proteins was higher when the extraction was carried out at pH 12 (17% for CPI12 and 13% for CPI10); however, CPI12 protein content (775 g/kg) was slightly lower than CPI10 protein content (782 g/kg). Both samples showed similar SDS-PAGE pattern. Protein dispersions of both isolates led to highly stabilized particles due to their negative ζ potential (around −54 mV). CPI10 has a higher proportion of small particles in suspension, revealed by a lower d3,2 value. Spectroscopic techniques showed that CPI10 presented higher content of β-helix than CPI12, resulting in higher thermal stability. This observation was supported by FT-IR spectroscopy since CPI10 presented less unordered structure than CPI12. The energy of endotherms obtained in CPI12 was considerably lower than in CPI10. Extraction at higher alkaline conditions led to a more denatured protein conformation with a higher content of random structure (18.1% for CPI10 and 22.9% for CPI12).
publishDate 2018
dc.date.none.fl_str_mv 2018-04
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/11336/93502
López, Débora Natalia; Ingrassia, Romina; Busti, Pablo Andres; Bonino, Julia; Delgado, Juan Francisco; et al.; “Structural characterization of protein isolates obtained from chia (Salvia hispanica L.) seeds”; Elsevier Science; LWT - Food Science and Technology; 90; 4-2018; 396-402
0023-6438
CONICET Digital
CONICET
url http://hdl.handle.net/11336/93502
identifier_str_mv López, Débora Natalia; Ingrassia, Romina; Busti, Pablo Andres; Bonino, Julia; Delgado, Juan Francisco; et al.; “Structural characterization of protein isolates obtained from chia (Salvia hispanica L.) seeds”; Elsevier Science; LWT - Food Science and Technology; 90; 4-2018; 396-402
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/doi/10.1016/j.lwt.2017.12.060
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0023643817309544
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
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
reponame_str 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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score 13.22299

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