Functionality of egg white proteins as affected by high intensity ultrasound

Autores
Arzeni, Carolina; Perez, Oscar Edgardo; Pilosof, Ana Maria Renata
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The goal of this contribution was to determine the impact of HIUS on the thermal aggregation, gelation, foaming and emulsifying properties of egg white (EW) proteins.EW solutions were sonicated for 20 min using an ultrasonic processor Vibra Cell Sonics, model VCX 750 (frequency: 20 kHz; amplitude: 20%). The following properties were determined: particle size distribution by light scattering, the dynamics of gelation upon time and temperature (70, 75, 80 and 85 °C), surface hydrophobicity, concentration of sulfhydryl (SH) groups, denaturation temperatures (Tpeak), bulk viscosity, foaming by a whipping method and emulsifying properties by the use of a vertical scan analyzer and droplet size determinations. In order to study aggregation, EW solutions were heated in a dry bath at 70, 75, 80 and 85 °C for different periods of time from 0 to 30 min and analyzed by static light scattering and confocal laser scanning microscopy.Surface hydrophobicity increased after sonication, but total SH content was not affected. The apparent viscosity decreased, which seemed to affect the stability of foams prepared with sonicated protein. Emulsions from sonicated samples resulted more stable to creaming and flocculation. The gelation temperature of EW did not vary substantially after sonication as well as the gelation properties studied. The rate of formation of aggregates upon heating was accelerated by sonication. This fact could be attributed to the increase in hydrophobicity of the protein. Thus, HIUS could allow improving some functional properties of EW.
Fil: Arzeni, Carolina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina
Fil: Perez, Oscar Edgardo. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Pilosof, Ana Maria Renata. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Materia
EGG WHITE PROTEIN
EMULSIFYING
FOAMING
GELATION
THERMAL AGGREGATION
ULTRASOUND
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:11336/189612
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/189612
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Functionality of egg white proteins as affected by high intensity ultrasoundArzeni, CarolinaPerez, Oscar EdgardoPilosof, Ana Maria RenataEGG WHITE PROTEINEMULSIFYINGFOAMINGGELATIONTHERMAL AGGREGATIONULTRASOUNDhttps://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2The goal of this contribution was to determine the impact of HIUS on the thermal aggregation, gelation, foaming and emulsifying properties of egg white (EW) proteins.EW solutions were sonicated for 20 min using an ultrasonic processor Vibra Cell Sonics, model VCX 750 (frequency: 20 kHz; amplitude: 20%). The following properties were determined: particle size distribution by light scattering, the dynamics of gelation upon time and temperature (70, 75, 80 and 85 °C), surface hydrophobicity, concentration of sulfhydryl (SH) groups, denaturation temperatures (Tpeak), bulk viscosity, foaming by a whipping method and emulsifying properties by the use of a vertical scan analyzer and droplet size determinations. In order to study aggregation, EW solutions were heated in a dry bath at 70, 75, 80 and 85 °C for different periods of time from 0 to 30 min and analyzed by static light scattering and confocal laser scanning microscopy.Surface hydrophobicity increased after sonication, but total SH content was not affected. The apparent viscosity decreased, which seemed to affect the stability of foams prepared with sonicated protein. Emulsions from sonicated samples resulted more stable to creaming and flocculation. The gelation temperature of EW did not vary substantially after sonication as well as the gelation properties studied. The rate of formation of aggregates upon heating was accelerated by sonication. This fact could be attributed to the increase in hydrophobicity of the protein. Thus, HIUS could allow improving some functional properties of EW.Fil: Arzeni, Carolina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; ArgentinaFil: Perez, Oscar Edgardo. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Pilosof, Ana Maria Renata. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaElsevier2012-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/189612Arzeni, Carolina; Perez, Oscar Edgardo; Pilosof, Ana Maria Renata; Functionality of egg white proteins as affected by high intensity ultrasound; Elsevier; Food Hydrocolloids; 29; 2; 12-2012; 308-3160268-005XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S0268005X12000690info:eu-repo/semantics/altIdentifier/doi/10.1016/j.foodhyd.2012.03.009info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:59:38Zoai:ri.conicet.gov.ar:11336/189612instacron: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:34982025-09-03 09:59:38.826CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Functionality of egg white proteins as affected by high intensity ultrasound
title Functionality of egg white proteins as affected by high intensity ultrasound
spellingShingle Functionality of egg white proteins as affected by high intensity ultrasound
Arzeni, Carolina
EGG WHITE PROTEIN
EMULSIFYING
FOAMING
GELATION
THERMAL AGGREGATION
ULTRASOUND
title_short Functionality of egg white proteins as affected by high intensity ultrasound
title_full Functionality of egg white proteins as affected by high intensity ultrasound
title_fullStr Functionality of egg white proteins as affected by high intensity ultrasound
title_full_unstemmed Functionality of egg white proteins as affected by high intensity ultrasound
title_sort Functionality of egg white proteins as affected by high intensity ultrasound
dc.creator.none.fl_str_mv Arzeni, Carolina
Perez, Oscar Edgardo
Pilosof, Ana Maria Renata
author Arzeni, Carolina
author_facet Arzeni, Carolina
Perez, Oscar Edgardo
Pilosof, Ana Maria Renata
author_role author
author2 Perez, Oscar Edgardo
Pilosof, Ana Maria Renata
author2_role author
author
dc.subject.none.fl_str_mv EGG WHITE PROTEIN
EMULSIFYING
FOAMING
GELATION
THERMAL AGGREGATION
ULTRASOUND
topic EGG WHITE PROTEIN
EMULSIFYING
FOAMING
GELATION
THERMAL AGGREGATION
ULTRASOUND
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 goal of this contribution was to determine the impact of HIUS on the thermal aggregation, gelation, foaming and emulsifying properties of egg white (EW) proteins.EW solutions were sonicated for 20 min using an ultrasonic processor Vibra Cell Sonics, model VCX 750 (frequency: 20 kHz; amplitude: 20%). The following properties were determined: particle size distribution by light scattering, the dynamics of gelation upon time and temperature (70, 75, 80 and 85 °C), surface hydrophobicity, concentration of sulfhydryl (SH) groups, denaturation temperatures (Tpeak), bulk viscosity, foaming by a whipping method and emulsifying properties by the use of a vertical scan analyzer and droplet size determinations. In order to study aggregation, EW solutions were heated in a dry bath at 70, 75, 80 and 85 °C for different periods of time from 0 to 30 min and analyzed by static light scattering and confocal laser scanning microscopy.Surface hydrophobicity increased after sonication, but total SH content was not affected. The apparent viscosity decreased, which seemed to affect the stability of foams prepared with sonicated protein. Emulsions from sonicated samples resulted more stable to creaming and flocculation. The gelation temperature of EW did not vary substantially after sonication as well as the gelation properties studied. The rate of formation of aggregates upon heating was accelerated by sonication. This fact could be attributed to the increase in hydrophobicity of the protein. Thus, HIUS could allow improving some functional properties of EW.
Fil: Arzeni, Carolina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina
Fil: Perez, Oscar Edgardo. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Pilosof, Ana Maria Renata. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
description The goal of this contribution was to determine the impact of HIUS on the thermal aggregation, gelation, foaming and emulsifying properties of egg white (EW) proteins.EW solutions were sonicated for 20 min using an ultrasonic processor Vibra Cell Sonics, model VCX 750 (frequency: 20 kHz; amplitude: 20%). The following properties were determined: particle size distribution by light scattering, the dynamics of gelation upon time and temperature (70, 75, 80 and 85 °C), surface hydrophobicity, concentration of sulfhydryl (SH) groups, denaturation temperatures (Tpeak), bulk viscosity, foaming by a whipping method and emulsifying properties by the use of a vertical scan analyzer and droplet size determinations. In order to study aggregation, EW solutions were heated in a dry bath at 70, 75, 80 and 85 °C for different periods of time from 0 to 30 min and analyzed by static light scattering and confocal laser scanning microscopy.Surface hydrophobicity increased after sonication, but total SH content was not affected. The apparent viscosity decreased, which seemed to affect the stability of foams prepared with sonicated protein. Emulsions from sonicated samples resulted more stable to creaming and flocculation. The gelation temperature of EW did not vary substantially after sonication as well as the gelation properties studied. The rate of formation of aggregates upon heating was accelerated by sonication. This fact could be attributed to the increase in hydrophobicity of the protein. Thus, HIUS could allow improving some functional properties of EW.
publishDate 2012
dc.date.none.fl_str_mv 2012-12
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/11336/189612
Arzeni, Carolina; Perez, Oscar Edgardo; Pilosof, Ana Maria Renata; Functionality of egg white proteins as affected by high intensity ultrasound; Elsevier; Food Hydrocolloids; 29; 2; 12-2012; 308-316
0268-005X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/189612
identifier_str_mv Arzeni, Carolina; Perez, Oscar Edgardo; Pilosof, Ana Maria Renata; Functionality of egg white proteins as affected by high intensity ultrasound; Elsevier; Food Hydrocolloids; 29; 2; 12-2012; 308-316
0268-005X
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/abs/pii/S0268005X12000690
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.foodhyd.2012.03.009
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
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 13.13397

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