Combination of pH-shifting, ultrasound, and heat treatments to enhance solubility and emulsifying stability of rice protein isolate

Autores
Igartúa, Daniela; Dichano, M. Celeste; Ferrari, Sofia B.; Palazolo, Gonzalo Gastón; Cabezas, Dario Marcelino
Año de publicación
2024
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Rice protein isolates (RPI) are promising plant-protein sources but present low solubility and poor surface activity in neutral conditions. Improving these characteristics is a crucial challenge to capitalize on them. This is the first work performing pH-shifting, ultrasound, and heat treatments on a commercial RPI. The combined approaches increased the protein solubility (from ~2.7% to ~91.8%) and surface hydrophobicity (up to ~283%) and induced the formation of less compact and more dispersed protein aggregates. The pH-shifting induced the unfolding of protein molecules and aggregates making them available for modification by both ultrasound and heating, which are supposed to induce further protein unfolding, exposure of buried hydrophobic amino acid, and protein hydrolysis. Also, the combined approaches generated modified RPI able to form oil-in-water emulsions with reduced particle size and enhanced stability than the untreated RPI. Therefore, this work presents an effective combined approach to enhance the techno-functional properties of rice proteins.
Fil: Igartúa, Daniela. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Área Ingeniería en Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Dichano, M. Celeste. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Área Ingeniería en Alimentos; Argentina
Fil: Ferrari, Sofia B.. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Área Ingeniería en Alimentos; Argentina
Fil: Palazolo, Gonzalo Gastón. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Área Ingeniería en Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Cabezas, Dario Marcelino. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Área Ingeniería en Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Materia
RICE PROTEINS
PH-SHIFTING
ULTRASOUND
HEAT TREATMENT
Nivel de accesibilidad
acceso embargado
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:11336/230737
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/230737
network_acronym_str CONICETDig
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network_name_str CONICET Digital (CONICET)
spelling Combination of pH-shifting, ultrasound, and heat treatments to enhance solubility and emulsifying stability of rice protein isolateIgartúa, DanielaDichano, M. CelesteFerrari, Sofia B.Palazolo, Gonzalo GastónCabezas, Dario MarcelinoRICE PROTEINSPH-SHIFTINGULTRASOUNDHEAT TREATMENThttps://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2Rice protein isolates (RPI) are promising plant-protein sources but present low solubility and poor surface activity in neutral conditions. Improving these characteristics is a crucial challenge to capitalize on them. This is the first work performing pH-shifting, ultrasound, and heat treatments on a commercial RPI. The combined approaches increased the protein solubility (from ~2.7% to ~91.8%) and surface hydrophobicity (up to ~283%) and induced the formation of less compact and more dispersed protein aggregates. The pH-shifting induced the unfolding of protein molecules and aggregates making them available for modification by both ultrasound and heating, which are supposed to induce further protein unfolding, exposure of buried hydrophobic amino acid, and protein hydrolysis. Also, the combined approaches generated modified RPI able to form oil-in-water emulsions with reduced particle size and enhanced stability than the untreated RPI. Therefore, this work presents an effective combined approach to enhance the techno-functional properties of rice proteins.Fil: Igartúa, Daniela. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Área Ingeniería en Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Dichano, M. Celeste. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Área Ingeniería en Alimentos; ArgentinaFil: Ferrari, Sofia B.. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Área Ingeniería en Alimentos; ArgentinaFil: Palazolo, Gonzalo Gastón. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Área Ingeniería en Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Cabezas, Dario Marcelino. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Área Ingeniería en Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaElsevier2024-02info:eu-repo/date/embargoEnd/2024-08-18info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/230737Igartúa, Daniela; Dichano, M. Celeste; Ferrari, Sofia B.; Palazolo, Gonzalo Gastón; Cabezas, Dario Marcelino; Combination of pH-shifting, ultrasound, and heat treatments to enhance solubility and emulsifying stability of rice protein isolate; Elsevier; Food Chemistry; 433; 2-2024; 1-230308-81461873-7072CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S0308814623019374info:eu-repo/semantics/altIdentifier/doi/10.1016/j.foodchem.2023.137319info:eu-repo/semantics/embargoedAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:00:51Zoai:ri.conicet.gov.ar:11336/230737instacron: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:34982025-10-22 11:00:51.811CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Combination of pH-shifting, ultrasound, and heat treatments to enhance solubility and emulsifying stability of rice protein isolate
title Combination of pH-shifting, ultrasound, and heat treatments to enhance solubility and emulsifying stability of rice protein isolate
spellingShingle Combination of pH-shifting, ultrasound, and heat treatments to enhance solubility and emulsifying stability of rice protein isolate
Igartúa, Daniela
RICE PROTEINS
PH-SHIFTING
ULTRASOUND
HEAT TREATMENT
title_short Combination of pH-shifting, ultrasound, and heat treatments to enhance solubility and emulsifying stability of rice protein isolate
title_full Combination of pH-shifting, ultrasound, and heat treatments to enhance solubility and emulsifying stability of rice protein isolate
title_fullStr Combination of pH-shifting, ultrasound, and heat treatments to enhance solubility and emulsifying stability of rice protein isolate
title_full_unstemmed Combination of pH-shifting, ultrasound, and heat treatments to enhance solubility and emulsifying stability of rice protein isolate
title_sort Combination of pH-shifting, ultrasound, and heat treatments to enhance solubility and emulsifying stability of rice protein isolate
dc.creator.none.fl_str_mv Igartúa, Daniela
Dichano, M. Celeste
Ferrari, Sofia B.
Palazolo, Gonzalo Gastón
Cabezas, Dario Marcelino
author Igartúa, Daniela
author_facet Igartúa, Daniela
Dichano, M. Celeste
Ferrari, Sofia B.
Palazolo, Gonzalo Gastón
Cabezas, Dario Marcelino
author_role author
author2 Dichano, M. Celeste
Ferrari, Sofia B.
Palazolo, Gonzalo Gastón
Cabezas, Dario Marcelino
author2_role author
author
author
author
dc.subject.none.fl_str_mv RICE PROTEINS
PH-SHIFTING
ULTRASOUND
HEAT TREATMENT
topic RICE PROTEINS
PH-SHIFTING
ULTRASOUND
HEAT TREATMENT
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.11
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv Rice protein isolates (RPI) are promising plant-protein sources but present low solubility and poor surface activity in neutral conditions. Improving these characteristics is a crucial challenge to capitalize on them. This is the first work performing pH-shifting, ultrasound, and heat treatments on a commercial RPI. The combined approaches increased the protein solubility (from ~2.7% to ~91.8%) and surface hydrophobicity (up to ~283%) and induced the formation of less compact and more dispersed protein aggregates. The pH-shifting induced the unfolding of protein molecules and aggregates making them available for modification by both ultrasound and heating, which are supposed to induce further protein unfolding, exposure of buried hydrophobic amino acid, and protein hydrolysis. Also, the combined approaches generated modified RPI able to form oil-in-water emulsions with reduced particle size and enhanced stability than the untreated RPI. Therefore, this work presents an effective combined approach to enhance the techno-functional properties of rice proteins.
Fil: Igartúa, Daniela. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Área Ingeniería en Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Dichano, M. Celeste. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Área Ingeniería en Alimentos; Argentina
Fil: Ferrari, Sofia B.. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Área Ingeniería en Alimentos; Argentina
Fil: Palazolo, Gonzalo Gastón. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Área Ingeniería en Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Cabezas, Dario Marcelino. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Área Ingeniería en Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
description Rice protein isolates (RPI) are promising plant-protein sources but present low solubility and poor surface activity in neutral conditions. Improving these characteristics is a crucial challenge to capitalize on them. This is the first work performing pH-shifting, ultrasound, and heat treatments on a commercial RPI. The combined approaches increased the protein solubility (from ~2.7% to ~91.8%) and surface hydrophobicity (up to ~283%) and induced the formation of less compact and more dispersed protein aggregates. The pH-shifting induced the unfolding of protein molecules and aggregates making them available for modification by both ultrasound and heating, which are supposed to induce further protein unfolding, exposure of buried hydrophobic amino acid, and protein hydrolysis. Also, the combined approaches generated modified RPI able to form oil-in-water emulsions with reduced particle size and enhanced stability than the untreated RPI. Therefore, this work presents an effective combined approach to enhance the techno-functional properties of rice proteins.
publishDate 2024
dc.date.none.fl_str_mv 2024-02
info:eu-repo/date/embargoEnd/2024-08-18
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/11336/230737
Igartúa, Daniela; Dichano, M. Celeste; Ferrari, Sofia B.; Palazolo, Gonzalo Gastón; Cabezas, Dario Marcelino; Combination of pH-shifting, ultrasound, and heat treatments to enhance solubility and emulsifying stability of rice protein isolate; Elsevier; Food Chemistry; 433; 2-2024; 1-23
0308-8146
1873-7072
CONICET Digital
CONICET
url http://hdl.handle.net/11336/230737
identifier_str_mv Igartúa, Daniela; Dichano, M. Celeste; Ferrari, Sofia B.; Palazolo, Gonzalo Gastón; Cabezas, Dario Marcelino; Combination of pH-shifting, ultrasound, and heat treatments to enhance solubility and emulsifying stability of rice protein isolate; Elsevier; Food Chemistry; 433; 2-2024; 1-23
0308-8146
1873-7072
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://linkinghub.elsevier.com/retrieve/pii/S0308814623019374
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.foodchem.2023.137319
dc.rights.none.fl_str_mv info:eu-repo/semantics/embargoedAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv embargoedAccess
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
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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 12.982451

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