Impact of high-pressure shift freezing on physicochemical and functional properties of egg edible parts

Effects of high-pressure shift freezing (HPSF) at 200 MPa/-20 °C on physical, functional and thermal properties of egg white and egg yolk from three egg types were studied. The phase transition time in HPSF was shorter compared to atmospheric freezing (about 25% for egg yolk and 56% for egg white) d...

Descripción completa

Detalles Bibliográficos
Autores: Dadashi, Saeed, Fernández Martín, Fernando, Mousavi, M., Pérez-Mateos, Miriam
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2023
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/335463
Acceso en línea:http://hdl.handle.net/10261/335463
Access Level:acceso abierto
Palabra clave:High-pressure shift freezing
Egg white
Egg yolk
Freezing processes
Thermal properties
Functional properties
id ES_7c3250e62c4e826c2cc92c00b7e32cd5
oai_identifier_str oai:digital.csic.es:10261/335463
network_acronym_str ES
network_name_str España
repository_id_str
spelling Impact of high-pressure shift freezing on physicochemical and functional properties of egg edible partsDadashi, SaeedFernández Martín, FernandoMousavi, M.Pérez-Mateos, MiriamHigh-pressure shift freezingEgg whiteEgg yolkFreezing processesThermal propertiesFunctional propertiesEffects of high-pressure shift freezing (HPSF) at 200 MPa/-20 °C on physical, functional and thermal properties of egg white and egg yolk from three egg types were studied. The phase transition time in HPSF was shorter compared to atmospheric freezing (about 25% for egg yolk and 56% for egg white) due to the high degree of supercooling. The effect of freezing on functional properties seems to be related to different degrees of protein denaturation depending of the freezing/pressure level. Partial protein unfolding (suggested by higher free sulfhydryl) was observed after freezing at atmospheric pressure, especially for egg yolk. On the other hand, higher protein aggregation due to lower thermal denaturation enthalpy (50% in egg yolk and 70% in egg white) was found in HPSF samples, supported by decrease of protein solubility, disappear of electrophoretic bands and increase in viscoelasticity (G′ and G″ values).This work was partially supported by the State Program to Promote Scientific-Technical Research and its Transfer of the Spanish Ministry of Science and Innovation through the MALTA CONSOLIDER TEAM Research Network (RED 2022-134388-T). S.D. acknowledges a Ph.D. Student fellowship from Iranian Ministry of Science.Peer reviewedElsevierMinisterio de Ciencia, Innovación y Universidades (España)Agencia Estatal de Investigación (España)Ministry of Science, Research, and Technology (Iran)Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]202320232024info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionapplication/pdfhttp://hdl.handle.net/10261/335463reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/AEI//RED2022-134388-TThe underlying dataset has been published as supplementary material of the article in the publisher platform at DOI 10.1016/j.jfoodeng.2023.111753https://doi.org/10.1016/j.jfoodeng.2023.111753Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/3354632026-05-22T06:33:51Z
dc.title.none.fl_str_mv Impact of high-pressure shift freezing on physicochemical and functional properties of egg edible parts
title Impact of high-pressure shift freezing on physicochemical and functional properties of egg edible parts
spellingShingle Impact of high-pressure shift freezing on physicochemical and functional properties of egg edible parts
Dadashi, Saeed
High-pressure shift freezing
Egg white
Egg yolk
Freezing processes
Thermal properties
Functional properties
title_short Impact of high-pressure shift freezing on physicochemical and functional properties of egg edible parts
title_full Impact of high-pressure shift freezing on physicochemical and functional properties of egg edible parts
title_fullStr Impact of high-pressure shift freezing on physicochemical and functional properties of egg edible parts
title_full_unstemmed Impact of high-pressure shift freezing on physicochemical and functional properties of egg edible parts
title_sort Impact of high-pressure shift freezing on physicochemical and functional properties of egg edible parts
dc.creator.none.fl_str_mv Dadashi, Saeed
Fernández Martín, Fernando
Mousavi, M.
Pérez-Mateos, Miriam
author Dadashi, Saeed
author_facet Dadashi, Saeed
Fernández Martín, Fernando
Mousavi, M.
Pérez-Mateos, Miriam
author_role author
author2 Fernández Martín, Fernando
Mousavi, M.
Pérez-Mateos, Miriam
author2_role author
author
author
dc.contributor.none.fl_str_mv Ministerio de Ciencia, Innovación y Universidades (España)
Agencia Estatal de Investigación (España)
Ministry of Science, Research, and Technology (Iran)
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv High-pressure shift freezing
Egg white
Egg yolk
Freezing processes
Thermal properties
Functional properties
topic High-pressure shift freezing
Egg white
Egg yolk
Freezing processes
Thermal properties
Functional properties
description Effects of high-pressure shift freezing (HPSF) at 200 MPa/-20 °C on physical, functional and thermal properties of egg white and egg yolk from three egg types were studied. The phase transition time in HPSF was shorter compared to atmospheric freezing (about 25% for egg yolk and 56% for egg white) due to the high degree of supercooling. The effect of freezing on functional properties seems to be related to different degrees of protein denaturation depending of the freezing/pressure level. Partial protein unfolding (suggested by higher free sulfhydryl) was observed after freezing at atmospheric pressure, especially for egg yolk. On the other hand, higher protein aggregation due to lower thermal denaturation enthalpy (50% in egg yolk and 70% in egg white) was found in HPSF samples, supported by decrease of protein solubility, disappear of electrophoretic bands and increase in viscoelasticity (G′ and G″ values).
publishDate 2023
dc.date.none.fl_str_mv 2023
2023
2024
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/335463
url http://hdl.handle.net/10261/335463
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv #PLACEHOLDER_PARENT_METADATA_VALUE#
info:eu-repo/grantAgreement/AEI//RED2022-134388-T
The underlying dataset has been published as supplementary material of the article in the publisher platform at DOI 10.1016/j.jfoodeng.2023.111753
https://doi.org/10.1016/j.jfoodeng.2023.111753
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869411572133134336
score 15.811543

Similares en LA Referencia