Physicochemical and functional properties of cowpea protein isolates treated with temperature or high hydrostatic pressure

Autores
Peyrano, Felicitas; Speroni Aguirre, Francisco José; Avanza, María Victoria
Año de publicación
2016
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Fil: Peyrano, Felicitas. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas y Naturales y Agrimensura; Argentina.
Fil: Peyrano, Felicitas. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina.
Fil: Speroni Aguirre, Francisco José. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina.
Fil: Speroni, Francisco J. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico; Argentina.
Fil: Avanza, María Victoria. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas y Naturales y Agrimensura; Argentina.
Fil: Avanza, María Victoria. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina.
The effect of thermal (TT, 70 and 90 °C) and high hydrostatic pressure (HHPTs, 200, 400 and 600MPa) treatments on physicochemical and functional properties of cowpea protein isolates (CPIs) extracted at pH 8.0 (A8) and pH 10.0 (A10)was analyzed. The pH of protein extraction affected some physicochemical properties (surface hydrophobicity (Ho) and denaturation temperature),without affecting the functional properties. Treatments led to the formation of soluble protein aggregates stabilized by disulfide bonds, especially with TT at 90 °C. TT and HHPTs shifted the wavelengths of maximum emission to red and to blue, respectively. All treatments induced unfolding and denaturation. HHPTs was more efficient than TT to enhance gelation andwater holding capacities. Interestingly, treated and untreated CPIs exhibited high values of solubility (72–97%). TT and HHPT induced greater changes in physicochemical and functional properties of A8 than in those of A10. Remarkably, functional properties were improved from the less energetic treatments (70 °C, 200 MPa).
Fuente
Innovative Food Science and Emerging Technologies, vol. 33, p. 38-46.
Materia
Legume protein
High hydrostatic pressure treatment
Thermal treatment
Cowpea protein isolate
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
Repositorio Institucional de la Universidad Nacional del Nordeste (UNNE)
Institución
Universidad Nacional del Nordeste
OAI Identificador
oai:repositorio.unne.edu.ar:123456789/28256
Acceder
id RIUNNE_fe316896c5f043b140376493dba2ff11
oai_identifier_str oai:repositorio.unne.edu.ar:123456789/28256
network_acronym_str RIUNNE
repository_id_str 4871
network_name_str Repositorio Institucional de la Universidad Nacional del Nordeste (UNNE)
spelling Physicochemical and functional properties of cowpea protein isolates treated with temperature or high hydrostatic pressurePeyrano, FelicitasSperoni Aguirre, Francisco JoséAvanza, María VictoriaLegume proteinHigh hydrostatic pressure treatmentThermal treatmentCowpea protein isolateFil: Peyrano, Felicitas. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas y Naturales y Agrimensura; Argentina.Fil: Peyrano, Felicitas. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina.Fil: Speroni Aguirre, Francisco José. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina.Fil: Speroni, Francisco J. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico; Argentina.Fil: Avanza, María Victoria. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas y Naturales y Agrimensura; Argentina.Fil: Avanza, María Victoria. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina.The effect of thermal (TT, 70 and 90 °C) and high hydrostatic pressure (HHPTs, 200, 400 and 600MPa) treatments on physicochemical and functional properties of cowpea protein isolates (CPIs) extracted at pH 8.0 (A8) and pH 10.0 (A10)was analyzed. The pH of protein extraction affected some physicochemical properties (surface hydrophobicity (Ho) and denaturation temperature),without affecting the functional properties. Treatments led to the formation of soluble protein aggregates stabilized by disulfide bonds, especially with TT at 90 °C. TT and HHPTs shifted the wavelengths of maximum emission to red and to blue, respectively. All treatments induced unfolding and denaturation. HHPTs was more efficient than TT to enhance gelation andwater holding capacities. Interestingly, treated and untreated CPIs exhibited high values of solubility (72–97%). TT and HHPT induced greater changes in physicochemical and functional properties of A8 than in those of A10. Remarkably, functional properties were improved from the less energetic treatments (70 °C, 200 MPa).Elsevier2016-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfPeyrano, Felicitas, Speroni Aguirre, Francisco José y Avanza María Victoria, 2016. Physicochemical and functional properties of cowpea protein isolates treated with temperature or high hydrostatic pressure. Innovative Food Science and Emerging Technologies. Elsevier: Ámsterdam, vol. 33, p. 38-46, ISSN 1466-8564.1466-8564http://repositorio.unne.edu.ar/handle/123456789/28256Innovative Food Science and Emerging Technologies, vol. 33, p. 38-46.reponame:Repositorio Institucional de la Universidad Nacional del Nordeste (UNNE)instname:Universidad Nacional del Nordesteenghttp://dx.doi.org/10.1016/j.ifset.2015.10.014http://dx.doi.org/10.1016/j.ifset.2015.10.014http://dx.doi.org/10.1016/j.ifset.2015.10.014info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-nd/2.5/ar/Atribución-NoComercial-SinDerivadas 2.5 Argentina2025-09-29T14:30:20Zoai:repositorio.unne.edu.ar:123456789/28256instacron:UNNEInstitucionalhttp://repositorio.unne.edu.ar/Universidad públicaNo correspondehttp://repositorio.unne.edu.ar/oaiososa@bib.unne.edu.ar;sergio.alegria@unne.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:48712025-09-29 14:30:21.185Repositorio Institucional de la Universidad Nacional del Nordeste (UNNE) - Universidad Nacional del Nordestefalse
dc.title.none.fl_str_mv Physicochemical and functional properties of cowpea protein isolates treated with temperature or high hydrostatic pressure
title Physicochemical and functional properties of cowpea protein isolates treated with temperature or high hydrostatic pressure
spellingShingle Physicochemical and functional properties of cowpea protein isolates treated with temperature or high hydrostatic pressure
Peyrano, Felicitas
Legume protein
High hydrostatic pressure treatment
Thermal treatment
Cowpea protein isolate
title_short Physicochemical and functional properties of cowpea protein isolates treated with temperature or high hydrostatic pressure
title_full Physicochemical and functional properties of cowpea protein isolates treated with temperature or high hydrostatic pressure
title_fullStr Physicochemical and functional properties of cowpea protein isolates treated with temperature or high hydrostatic pressure
title_full_unstemmed Physicochemical and functional properties of cowpea protein isolates treated with temperature or high hydrostatic pressure
title_sort Physicochemical and functional properties of cowpea protein isolates treated with temperature or high hydrostatic pressure
dc.creator.none.fl_str_mv Peyrano, Felicitas
Speroni Aguirre, Francisco José
Avanza, María Victoria
author Peyrano, Felicitas
author_facet Peyrano, Felicitas
Speroni Aguirre, Francisco José
Avanza, María Victoria
author_role author
author2 Speroni Aguirre, Francisco José
Avanza, María Victoria
author2_role author
author
dc.subject.none.fl_str_mv Legume protein
High hydrostatic pressure treatment
Thermal treatment
Cowpea protein isolate
topic Legume protein
High hydrostatic pressure treatment
Thermal treatment
Cowpea protein isolate
dc.description.none.fl_txt_mv Fil: Peyrano, Felicitas. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas y Naturales y Agrimensura; Argentina.
Fil: Peyrano, Felicitas. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina.
Fil: Speroni Aguirre, Francisco José. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina.
Fil: Speroni, Francisco J. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico; Argentina.
Fil: Avanza, María Victoria. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas y Naturales y Agrimensura; Argentina.
Fil: Avanza, María Victoria. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina.
The effect of thermal (TT, 70 and 90 °C) and high hydrostatic pressure (HHPTs, 200, 400 and 600MPa) treatments on physicochemical and functional properties of cowpea protein isolates (CPIs) extracted at pH 8.0 (A8) and pH 10.0 (A10)was analyzed. The pH of protein extraction affected some physicochemical properties (surface hydrophobicity (Ho) and denaturation temperature),without affecting the functional properties. Treatments led to the formation of soluble protein aggregates stabilized by disulfide bonds, especially with TT at 90 °C. TT and HHPTs shifted the wavelengths of maximum emission to red and to blue, respectively. All treatments induced unfolding and denaturation. HHPTs was more efficient than TT to enhance gelation andwater holding capacities. Interestingly, treated and untreated CPIs exhibited high values of solubility (72–97%). TT and HHPT induced greater changes in physicochemical and functional properties of A8 than in those of A10. Remarkably, functional properties were improved from the less energetic treatments (70 °C, 200 MPa).
description Fil: Peyrano, Felicitas. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas y Naturales y Agrimensura; Argentina.
publishDate 2016
dc.date.none.fl_str_mv 2016-02
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 Peyrano, Felicitas, Speroni Aguirre, Francisco José y Avanza María Victoria, 2016. Physicochemical and functional properties of cowpea protein isolates treated with temperature or high hydrostatic pressure. Innovative Food Science and Emerging Technologies. Elsevier: Ámsterdam, vol. 33, p. 38-46, ISSN 1466-8564.
1466-8564
http://repositorio.unne.edu.ar/handle/123456789/28256
identifier_str_mv Peyrano, Felicitas, Speroni Aguirre, Francisco José y Avanza María Victoria, 2016. Physicochemical and functional properties of cowpea protein isolates treated with temperature or high hydrostatic pressure. Innovative Food Science and Emerging Technologies. Elsevier: Ámsterdam, vol. 33, p. 38-46, ISSN 1466-8564.
1466-8564
url http://repositorio.unne.edu.ar/handle/123456789/28256
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv http://dx.doi.org/10.1016/j.ifset.2015.10.014
http://dx.doi.org/10.1016/j.ifset.2015.10.014
http://dx.doi.org/10.1016/j.ifset.2015.10.014
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Atribución-NoComercial-SinDerivadas 2.5 Argentina
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Atribución-NoComercial-SinDerivadas 2.5 Argentina
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv Innovative Food Science and Emerging Technologies, vol. 33, p. 38-46.
reponame:Repositorio Institucional de la Universidad Nacional del Nordeste (UNNE)
instname:Universidad Nacional del Nordeste
reponame_str Repositorio Institucional de la Universidad Nacional del Nordeste (UNNE)
collection Repositorio Institucional de la Universidad Nacional del Nordeste (UNNE)
instname_str Universidad Nacional del Nordeste
repository.name.fl_str_mv Repositorio Institucional de la Universidad Nacional del Nordeste (UNNE) - Universidad Nacional del Nordeste
repository.mail.fl_str_mv ososa@bib.unne.edu.ar;sergio.alegria@unne.edu.ar
_version_ 1844621687855775744
score 12.749369

Publicaciones similares