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
- Institución
- Universidad Nacional de La Plata
- OAI Identificador
- oai:sedici.unlp.edu.ar:10915/144142
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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 |
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SEDICI (UNLP) |
instname_str |
Universidad Nacional de La Plata |
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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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score |
13.001348 |