Calorimetric study of cowpea protein isolates: effect of calcium and high hydrostatic pressure

Autores
Peyrano, Felicitas; de Lamballerie, Marie; Avanza, María Victoria; Speroni Aguirre, Francisco
Año de publicación
2017
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The thermal properties of cowpea protein isolates (CPI) were studied by differential scanning calorimetry under the influence of various conditions. An increase in the pH of protein extraction, from 8.0 to 10.0, during CPI preparation promoted a partial denaturation of cowpea proteins. Increases in enthalpy change of denaturation (ΔH) and temperature of denaturation (Td) were detected with increasing protein concentration from 7.5 to 10.5% (w/w). This behavior suggests that denaturation involves a first step of dissociation of protein aggregates. Calcium induced thermal stabilization in cowpea proteins, the increase in Td was ca. 0.3 °C/mM for protein dispersions of 7.5% (w/w) for 0 to 40 mM CaCl2. High hydrostatic pressure (HHP) induced denaturation in CPI in a pressure level dependent manner. The presence of calcium protected cowpea proteins towards HHP-induced denaturation when pressure level was 400 MPa, but not when it was 600 MPa. Thermal properties of cowpea protein isolates were very sensitive to processing conditions, these behaviors would have implications in processing of CPI-containing foodstuff.
Centro de Investigación y Desarrollo en Criotecnología de Alimentos
Materia
Química
Cowpea proteins
DSC
Protein denaturation
Baroprotection
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/144142

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oai_identifier_str oai:sedici.unlp.edu.ar:10915/144142
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Calorimetric study of cowpea protein isolates: effect of calcium and high hydrostatic pressurePeyrano, Felicitasde Lamballerie, MarieAvanza, María VictoriaSperoni Aguirre, FranciscoQuímicaCowpea proteinsDSCProtein denaturationBaroprotectionThe thermal properties of cowpea protein isolates (CPI) were studied by differential scanning calorimetry under the influence of various conditions. An increase in the pH of protein extraction, from 8.0 to 10.0, during CPI preparation promoted a partial denaturation of cowpea proteins. Increases in enthalpy change of denaturation (ΔH) and temperature of denaturation (Td) were detected with increasing protein concentration from 7.5 to 10.5% (w/w). This behavior suggests that denaturation involves a first step of dissociation of protein aggregates. Calcium induced thermal stabilization in cowpea proteins, the increase in Td was ca. 0.3 °C/mM for protein dispersions of 7.5% (w/w) for 0 to 40 mM CaCl2. High hydrostatic pressure (HHP) induced denaturation in CPI in a pressure level dependent manner. The presence of calcium protected cowpea proteins towards HHP-induced denaturation when pressure level was 400 MPa, but not when it was 600 MPa. Thermal properties of cowpea protein isolates were very sensitive to processing conditions, these behaviors would have implications in processing of CPI-containing foodstuff.Centro de Investigación y Desarrollo en Criotecnología de Alimentos2017info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf374-382http://sedici.unlp.edu.ar/handle/10915/144142enginfo:eu-repo/semantics/altIdentifier/issn/1557-1858info:eu-repo/semantics/altIdentifier/issn/1557-1866info:eu-repo/semantics/altIdentifier/doi/10.1007/s11483-017-9493-4info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-17T10:15:10Zoai:sedici.unlp.edu.ar:10915/144142Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-17 10:15:10.294SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Calorimetric study of cowpea protein isolates: effect of calcium and high hydrostatic pressure
title Calorimetric study of cowpea protein isolates: effect of calcium and high hydrostatic pressure
spellingShingle Calorimetric study of cowpea protein isolates: effect of calcium and high hydrostatic pressure
Peyrano, Felicitas
Química
Cowpea proteins
DSC
Protein denaturation
Baroprotection
title_short Calorimetric study of cowpea protein isolates: effect of calcium and high hydrostatic pressure
title_full Calorimetric study of cowpea protein isolates: effect of calcium and high hydrostatic pressure
title_fullStr Calorimetric study of cowpea protein isolates: effect of calcium and high hydrostatic pressure
title_full_unstemmed Calorimetric study of cowpea protein isolates: effect of calcium and high hydrostatic pressure
title_sort Calorimetric study of cowpea protein isolates: effect of calcium and high hydrostatic pressure
dc.creator.none.fl_str_mv Peyrano, Felicitas
de Lamballerie, Marie
Avanza, María Victoria
Speroni Aguirre, Francisco
author Peyrano, Felicitas
author_facet Peyrano, Felicitas
de Lamballerie, Marie
Avanza, María Victoria
Speroni Aguirre, Francisco
author_role author
author2 de Lamballerie, Marie
Avanza, María Victoria
Speroni Aguirre, Francisco
author2_role author
author
author
dc.subject.none.fl_str_mv Química
Cowpea proteins
DSC
Protein denaturation
Baroprotection
topic Química
Cowpea proteins
DSC
Protein denaturation
Baroprotection
dc.description.none.fl_txt_mv The thermal properties of cowpea protein isolates (CPI) were studied by differential scanning calorimetry under the influence of various conditions. An increase in the pH of protein extraction, from 8.0 to 10.0, during CPI preparation promoted a partial denaturation of cowpea proteins. Increases in enthalpy change of denaturation (ΔH) and temperature of denaturation (Td) were detected with increasing protein concentration from 7.5 to 10.5% (w/w). This behavior suggests that denaturation involves a first step of dissociation of protein aggregates. Calcium induced thermal stabilization in cowpea proteins, the increase in Td was ca. 0.3 °C/mM for protein dispersions of 7.5% (w/w) for 0 to 40 mM CaCl2. High hydrostatic pressure (HHP) induced denaturation in CPI in a pressure level dependent manner. The presence of calcium protected cowpea proteins towards HHP-induced denaturation when pressure level was 400 MPa, but not when it was 600 MPa. Thermal properties of cowpea protein isolates were very sensitive to processing conditions, these behaviors would have implications in processing of CPI-containing foodstuff.
Centro de Investigación y Desarrollo en Criotecnología de Alimentos
description The thermal properties of cowpea protein isolates (CPI) were studied by differential scanning calorimetry under the influence of various conditions. An increase in the pH of protein extraction, from 8.0 to 10.0, during CPI preparation promoted a partial denaturation of cowpea proteins. Increases in enthalpy change of denaturation (ΔH) and temperature of denaturation (Td) were detected with increasing protein concentration from 7.5 to 10.5% (w/w). This behavior suggests that denaturation involves a first step of dissociation of protein aggregates. Calcium induced thermal stabilization in cowpea proteins, the increase in Td was ca. 0.3 °C/mM for protein dispersions of 7.5% (w/w) for 0 to 40 mM CaCl2. High hydrostatic pressure (HHP) induced denaturation in CPI in a pressure level dependent manner. The presence of calcium protected cowpea proteins towards HHP-induced denaturation when pressure level was 400 MPa, but not when it was 600 MPa. Thermal properties of cowpea protein isolates were very sensitive to processing conditions, these behaviors would have implications in processing of CPI-containing foodstuff.
publishDate 2017
dc.date.none.fl_str_mv 2017
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
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://sedici.unlp.edu.ar/handle/10915/144142
url http://sedici.unlp.edu.ar/handle/10915/144142
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/1557-1858
info:eu-repo/semantics/altIdentifier/issn/1557-1866
info:eu-repo/semantics/altIdentifier/doi/10.1007/s11483-017-9493-4
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
374-382
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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