Acid-induced aggregation and gelation of heat-treated chia proteins
- Autores
- López, Débora Natalia; Ingrassia, Romina; Busti, Pablo Andres; Wagner, Jorge Ricardo; Boeris, Valeria; Spelzini, Darío
- Año de publicación
- 2021
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- This work studied for the first time the acid-induced aggregation and gelation of heat-treated chia protein isolates obtained by extraction at pH 10 or 12 (CPI10 and CPI12, respectively). The aggregation state of proteins was modified during acidification. The size of the aggregates was reduced for both samples when the pH decreased but below pH 4.5 further protein aggregation took place for CPI12. Gelation of CPI12 was completed after about 30 min of acidification with glucone-δ-lactone. By contrast, this period was not enough to reach a constant value in G′ for CPI10. When gelation was ensured, confocal laser scanning micrographs from those gels revealed a coarse and irregular structure with large pores (median size of diameters: 30 μm). Instead, micrographs from CPI12 cold gels showed a more regular and interconnected network, with smaller pores (median size of diameters: 9 μm). These differences are consistent with a higher elastic behaviour ((Formula presented.) = 13.6 ± 0.1 Pa).
Fil: López, Débora Natalia. 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. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina
Fil: Ingrassia, Romina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Veterinarias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina
Fil: Busti, Pablo Andres. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; Argentina
Fil: Wagner, Jorge Ricardo. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Boeris, Valeria. 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. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina
Fil: Spelzini, Darío. 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. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina - Materia
-
ACIDIFIED SYSTEMS
COLD-SET GELATION
GLUCONE-Δ-LACTONE
SALVIA HISPANICA L - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/151099
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Acid-induced aggregation and gelation of heat-treated chia proteinsLópez, Débora NataliaIngrassia, RominaBusti, Pablo AndresWagner, Jorge RicardoBoeris, ValeriaSpelzini, DaríoACIDIFIED SYSTEMSCOLD-SET GELATIONGLUCONE-Δ-LACTONESALVIA HISPANICA Lhttps://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2This work studied for the first time the acid-induced aggregation and gelation of heat-treated chia protein isolates obtained by extraction at pH 10 or 12 (CPI10 and CPI12, respectively). The aggregation state of proteins was modified during acidification. The size of the aggregates was reduced for both samples when the pH decreased but below pH 4.5 further protein aggregation took place for CPI12. Gelation of CPI12 was completed after about 30 min of acidification with glucone-δ-lactone. By contrast, this period was not enough to reach a constant value in G′ for CPI10. When gelation was ensured, confocal laser scanning micrographs from those gels revealed a coarse and irregular structure with large pores (median size of diameters: 30 μm). Instead, micrographs from CPI12 cold gels showed a more regular and interconnected network, with smaller pores (median size of diameters: 9 μm). These differences are consistent with a higher elastic behaviour ((Formula presented.) = 13.6 ± 0.1 Pa).Fil: López, Débora Natalia. 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. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; ArgentinaFil: Ingrassia, Romina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Veterinarias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; ArgentinaFil: Busti, Pablo Andres. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; ArgentinaFil: Wagner, Jorge Ricardo. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Boeris, Valeria. 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. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; ArgentinaFil: Spelzini, Darío. 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. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; ArgentinaWiley Blackwell Publishing, Inc2021-04info: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/11336/151099López, Débora Natalia; Ingrassia, Romina; Busti, Pablo Andres; Wagner, Jorge Ricardo; Boeris, Valeria; et al.; Acid-induced aggregation and gelation of heat-treated chia proteins; Wiley Blackwell Publishing, Inc; International Journal of Food Science and Technology; 56; 4; 4-2021; 1641-16480950-54231365-2621CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/10.1111/ijfs.14784info:eu-repo/semantics/altIdentifier/doi/10.1111/ijfs.14784info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:11:39Zoai:ri.conicet.gov.ar:11336/151099instacron: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 10:11:39.437CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Acid-induced aggregation and gelation of heat-treated chia proteins |
title |
Acid-induced aggregation and gelation of heat-treated chia proteins |
spellingShingle |
Acid-induced aggregation and gelation of heat-treated chia proteins López, Débora Natalia ACIDIFIED SYSTEMS COLD-SET GELATION GLUCONE-Δ-LACTONE SALVIA HISPANICA L |
title_short |
Acid-induced aggregation and gelation of heat-treated chia proteins |
title_full |
Acid-induced aggregation and gelation of heat-treated chia proteins |
title_fullStr |
Acid-induced aggregation and gelation of heat-treated chia proteins |
title_full_unstemmed |
Acid-induced aggregation and gelation of heat-treated chia proteins |
title_sort |
Acid-induced aggregation and gelation of heat-treated chia proteins |
dc.creator.none.fl_str_mv |
López, Débora Natalia Ingrassia, Romina Busti, Pablo Andres Wagner, Jorge Ricardo Boeris, Valeria Spelzini, Darío |
author |
López, Débora Natalia |
author_facet |
López, Débora Natalia Ingrassia, Romina Busti, Pablo Andres Wagner, Jorge Ricardo Boeris, Valeria Spelzini, Darío |
author_role |
author |
author2 |
Ingrassia, Romina Busti, Pablo Andres Wagner, Jorge Ricardo Boeris, Valeria Spelzini, Darío |
author2_role |
author author author author author |
dc.subject.none.fl_str_mv |
ACIDIFIED SYSTEMS COLD-SET GELATION GLUCONE-Δ-LACTONE SALVIA HISPANICA L |
topic |
ACIDIFIED SYSTEMS COLD-SET GELATION GLUCONE-Δ-LACTONE SALVIA HISPANICA L |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/2.11 https://purl.org/becyt/ford/2 |
dc.description.none.fl_txt_mv |
This work studied for the first time the acid-induced aggregation and gelation of heat-treated chia protein isolates obtained by extraction at pH 10 or 12 (CPI10 and CPI12, respectively). The aggregation state of proteins was modified during acidification. The size of the aggregates was reduced for both samples when the pH decreased but below pH 4.5 further protein aggregation took place for CPI12. Gelation of CPI12 was completed after about 30 min of acidification with glucone-δ-lactone. By contrast, this period was not enough to reach a constant value in G′ for CPI10. When gelation was ensured, confocal laser scanning micrographs from those gels revealed a coarse and irregular structure with large pores (median size of diameters: 30 μm). Instead, micrographs from CPI12 cold gels showed a more regular and interconnected network, with smaller pores (median size of diameters: 9 μm). These differences are consistent with a higher elastic behaviour ((Formula presented.) = 13.6 ± 0.1 Pa). Fil: López, Débora Natalia. 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. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina Fil: Ingrassia, Romina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Veterinarias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina Fil: Busti, Pablo Andres. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; Argentina Fil: Wagner, Jorge Ricardo. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Boeris, Valeria. 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. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina Fil: Spelzini, Darío. 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. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina |
description |
This work studied for the first time the acid-induced aggregation and gelation of heat-treated chia protein isolates obtained by extraction at pH 10 or 12 (CPI10 and CPI12, respectively). The aggregation state of proteins was modified during acidification. The size of the aggregates was reduced for both samples when the pH decreased but below pH 4.5 further protein aggregation took place for CPI12. Gelation of CPI12 was completed after about 30 min of acidification with glucone-δ-lactone. By contrast, this period was not enough to reach a constant value in G′ for CPI10. When gelation was ensured, confocal laser scanning micrographs from those gels revealed a coarse and irregular structure with large pores (median size of diameters: 30 μm). Instead, micrographs from CPI12 cold gels showed a more regular and interconnected network, with smaller pores (median size of diameters: 9 μm). These differences are consistent with a higher elastic behaviour ((Formula presented.) = 13.6 ± 0.1 Pa). |
publishDate |
2021 |
dc.date.none.fl_str_mv |
2021-04 |
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/11336/151099 López, Débora Natalia; Ingrassia, Romina; Busti, Pablo Andres; Wagner, Jorge Ricardo; Boeris, Valeria; et al.; Acid-induced aggregation and gelation of heat-treated chia proteins; Wiley Blackwell Publishing, Inc; International Journal of Food Science and Technology; 56; 4; 4-2021; 1641-1648 0950-5423 1365-2621 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/151099 |
identifier_str_mv |
López, Débora Natalia; Ingrassia, Romina; Busti, Pablo Andres; Wagner, Jorge Ricardo; Boeris, Valeria; et al.; Acid-induced aggregation and gelation of heat-treated chia proteins; Wiley Blackwell Publishing, Inc; International Journal of Food Science and Technology; 56; 4; 4-2021; 1641-1648 0950-5423 1365-2621 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://onlinelibrary.wiley.com/doi/10.1111/ijfs.14784 info:eu-repo/semantics/altIdentifier/doi/10.1111/ijfs.14784 |
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 |
dc.publisher.none.fl_str_mv |
Wiley Blackwell Publishing, Inc |
publisher.none.fl_str_mv |
Wiley Blackwell Publishing, Inc |
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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1844614017521287168 |
score |
13.070432 |