Differential scanning calorimetry (DSC) studies on the thermal properties of peanut proteins

Autores
Colombo, Andrés; Ribotta, Pablo Daniel; Leon, Alberto Edel
Año de publicación
2010
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Studies related to the functional and thermal properties of peanut proteins are limited if compared with other vegetable protein sources. The aim of this work was to study the thermal denaturation of peanut protein isolates (PPI) by DSC. The thermal profile of PPI showed two endothermic peaks (assigned to denaturation of arachin and conarachin fractions). The thermal stability of arachin and conarachin increased when water content decreased, and a critical water level was found for both fractions. The effect of protein denaturants was studied. Low contents of urea stabilized protein fractions, but lower T d values were found with increasing concentrations. δH values of arachin were affected by urea. SDS affected δH values and thermal stability of conarachin; the arachin fraction showed higher resistance to SDS-induced denaturation. DTT addition did not affect conarachin stability, although enthalpy values decreased significantly. On the other hand, arachin was greatly affected by DTT. In summary, thermal denaturation parameters of PPI were sensitive to water content, indicating that polar groups of arachin and conarachin contribute to structure stabilization. Urea addition mainly affected the structure of the arachin fraction, which was attributed to its higher surface hydrophobicity. Results obtained from SDS and DTT suggest that hydrophobic interactions and disulfide bonds play an important role in structure maintenance of arachin and conarachin.
Fil: Colombo, Andrés. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Ciencia y Tecnología de Alimentos Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Ciencia y Tecnología de Alimentos Córdoba; Argentina
Fil: Ribotta, Pablo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Ciencia y Tecnología de Alimentos Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Ciencia y Tecnología de Alimentos Córdoba; Argentina
Fil: Leon, Alberto Edel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Ciencia y Tecnología de Alimentos Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Ciencia y Tecnología de Alimentos Córdoba; Argentina
Materia
DSC
PEANUT
PROTEIN DENATURANTS
PROTEINS
THERMAL DENATURATION
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:11336/187681
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/187681
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Differential scanning calorimetry (DSC) studies on the thermal properties of peanut proteinsColombo, AndrésRibotta, Pablo DanielLeon, Alberto EdelDSCPEANUTPROTEIN DENATURANTSPROTEINSTHERMAL DENATURATIONhttps://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2Studies related to the functional and thermal properties of peanut proteins are limited if compared with other vegetable protein sources. The aim of this work was to study the thermal denaturation of peanut protein isolates (PPI) by DSC. The thermal profile of PPI showed two endothermic peaks (assigned to denaturation of arachin and conarachin fractions). The thermal stability of arachin and conarachin increased when water content decreased, and a critical water level was found for both fractions. The effect of protein denaturants was studied. Low contents of urea stabilized protein fractions, but lower T d values were found with increasing concentrations. δH values of arachin were affected by urea. SDS affected δH values and thermal stability of conarachin; the arachin fraction showed higher resistance to SDS-induced denaturation. DTT addition did not affect conarachin stability, although enthalpy values decreased significantly. On the other hand, arachin was greatly affected by DTT. In summary, thermal denaturation parameters of PPI were sensitive to water content, indicating that polar groups of arachin and conarachin contribute to structure stabilization. Urea addition mainly affected the structure of the arachin fraction, which was attributed to its higher surface hydrophobicity. Results obtained from SDS and DTT suggest that hydrophobic interactions and disulfide bonds play an important role in structure maintenance of arachin and conarachin.Fil: Colombo, Andrés. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Ciencia y Tecnología de Alimentos Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Ciencia y Tecnología de Alimentos Córdoba; ArgentinaFil: Ribotta, Pablo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Ciencia y Tecnología de Alimentos Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Ciencia y Tecnología de Alimentos Córdoba; ArgentinaFil: Leon, Alberto Edel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Ciencia y Tecnología de Alimentos Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Ciencia y Tecnología de Alimentos Córdoba; ArgentinaAmerican Chemical Society2010-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/187681Colombo, Andrés; Ribotta, Pablo Daniel; Leon, Alberto Edel; Differential scanning calorimetry (DSC) studies on the thermal properties of peanut proteins; American Chemical Society; Journal of Agricultural and Food Chemistry; 58; 7; 4-2010; 4434-44390021-85611520-5118CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/10.1021/jf903426finfo:eu-repo/semantics/altIdentifier/doi/10.1021/jf903426finfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:55:05Zoai:ri.conicet.gov.ar:11336/187681instacron: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:34982025-10-22 11:55:06.122CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Differential scanning calorimetry (DSC) studies on the thermal properties of peanut proteins
title Differential scanning calorimetry (DSC) studies on the thermal properties of peanut proteins
spellingShingle Differential scanning calorimetry (DSC) studies on the thermal properties of peanut proteins
Colombo, Andrés
DSC
PEANUT
PROTEIN DENATURANTS
PROTEINS
THERMAL DENATURATION
title_short Differential scanning calorimetry (DSC) studies on the thermal properties of peanut proteins
title_full Differential scanning calorimetry (DSC) studies on the thermal properties of peanut proteins
title_fullStr Differential scanning calorimetry (DSC) studies on the thermal properties of peanut proteins
title_full_unstemmed Differential scanning calorimetry (DSC) studies on the thermal properties of peanut proteins
title_sort Differential scanning calorimetry (DSC) studies on the thermal properties of peanut proteins
dc.creator.none.fl_str_mv Colombo, Andrés
Ribotta, Pablo Daniel
Leon, Alberto Edel
author Colombo, Andrés
author_facet Colombo, Andrés
Ribotta, Pablo Daniel
Leon, Alberto Edel
author_role author
author2 Ribotta, Pablo Daniel
Leon, Alberto Edel
author2_role author
author
dc.subject.none.fl_str_mv DSC
PEANUT
PROTEIN DENATURANTS
PROTEINS
THERMAL DENATURATION
topic DSC
PEANUT
PROTEIN DENATURANTS
PROTEINS
THERMAL DENATURATION
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.11
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv Studies related to the functional and thermal properties of peanut proteins are limited if compared with other vegetable protein sources. The aim of this work was to study the thermal denaturation of peanut protein isolates (PPI) by DSC. The thermal profile of PPI showed two endothermic peaks (assigned to denaturation of arachin and conarachin fractions). The thermal stability of arachin and conarachin increased when water content decreased, and a critical water level was found for both fractions. The effect of protein denaturants was studied. Low contents of urea stabilized protein fractions, but lower T d values were found with increasing concentrations. δH values of arachin were affected by urea. SDS affected δH values and thermal stability of conarachin; the arachin fraction showed higher resistance to SDS-induced denaturation. DTT addition did not affect conarachin stability, although enthalpy values decreased significantly. On the other hand, arachin was greatly affected by DTT. In summary, thermal denaturation parameters of PPI were sensitive to water content, indicating that polar groups of arachin and conarachin contribute to structure stabilization. Urea addition mainly affected the structure of the arachin fraction, which was attributed to its higher surface hydrophobicity. Results obtained from SDS and DTT suggest that hydrophobic interactions and disulfide bonds play an important role in structure maintenance of arachin and conarachin.
Fil: Colombo, Andrés. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Ciencia y Tecnología de Alimentos Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Ciencia y Tecnología de Alimentos Córdoba; Argentina
Fil: Ribotta, Pablo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Ciencia y Tecnología de Alimentos Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Ciencia y Tecnología de Alimentos Córdoba; Argentina
Fil: Leon, Alberto Edel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Ciencia y Tecnología de Alimentos Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Ciencia y Tecnología de Alimentos Córdoba; Argentina
description Studies related to the functional and thermal properties of peanut proteins are limited if compared with other vegetable protein sources. The aim of this work was to study the thermal denaturation of peanut protein isolates (PPI) by DSC. The thermal profile of PPI showed two endothermic peaks (assigned to denaturation of arachin and conarachin fractions). The thermal stability of arachin and conarachin increased when water content decreased, and a critical water level was found for both fractions. The effect of protein denaturants was studied. Low contents of urea stabilized protein fractions, but lower T d values were found with increasing concentrations. δH values of arachin were affected by urea. SDS affected δH values and thermal stability of conarachin; the arachin fraction showed higher resistance to SDS-induced denaturation. DTT addition did not affect conarachin stability, although enthalpy values decreased significantly. On the other hand, arachin was greatly affected by DTT. In summary, thermal denaturation parameters of PPI were sensitive to water content, indicating that polar groups of arachin and conarachin contribute to structure stabilization. Urea addition mainly affected the structure of the arachin fraction, which was attributed to its higher surface hydrophobicity. Results obtained from SDS and DTT suggest that hydrophobic interactions and disulfide bonds play an important role in structure maintenance of arachin and conarachin.
publishDate 2010
dc.date.none.fl_str_mv 2010-04
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/11336/187681
Colombo, Andrés; Ribotta, Pablo Daniel; Leon, Alberto Edel; Differential scanning calorimetry (DSC) studies on the thermal properties of peanut proteins; American Chemical Society; Journal of Agricultural and Food Chemistry; 58; 7; 4-2010; 4434-4439
0021-8561
1520-5118
CONICET Digital
CONICET
url http://hdl.handle.net/11336/187681
identifier_str_mv Colombo, Andrés; Ribotta, Pablo Daniel; Leon, Alberto Edel; Differential scanning calorimetry (DSC) studies on the thermal properties of peanut proteins; American Chemical Society; Journal of Agricultural and Food Chemistry; 58; 7; 4-2010; 4434-4439
0021-8561
1520-5118
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://pubs.acs.org/doi/10.1021/jf903426f
info:eu-repo/semantics/altIdentifier/doi/10.1021/jf903426f
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
application/pdf
dc.publisher.none.fl_str_mv American Chemical Society
publisher.none.fl_str_mv American Chemical Society
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 12.982451

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