Characterization of soybean protein isolates : The effect of calcium presence
- Autores
- Scilingo, Adriana Alicia; Añón, María Cristina
- Año de publicación
- 2004
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Results of a study of the effect of calcium addition on polypeptide composition, hydrophobicity, sulfhydryl content, thermal stability, enthalpy of denaturation, and water solubility of soybean protein isolates suggest that the addition of small amounts of calcium (1.23–5.0 mg/g protein) induced the formation of α, α′ soluble aggregates, whereas large amounts (5.0–9.73 mg/g protein) induced the selective insolubilization of the glycinin fraction. The addition of this ion also produced thermal stabilization of the soybean proteins, mainly the glycinin fraction, and increased the enthalpy of denaturation. A decrease in the surface hydrophobicity of proteins with increasing calcium content was also observed. The results obtained suggested the existence of specific calcium-soy protein interactions, especially with the glycinin fraction.
Centro de Investigación y Desarrollo en Criotecnología de Alimentos - Materia
-
Ciencias Exactas
Química
Calcium addition
solubility
soybean protein isolates - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- http://creativecommons.org/licenses/by/4.0/
- Repositorio
- Institución
- Universidad Nacional de La Plata
- OAI Identificador
- oai:sedici.unlp.edu.ar:10915/138658
Ver los metadatos del registro completo
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Characterization of soybean protein isolates : The effect of calcium presenceScilingo, Adriana AliciaAñón, María CristinaCiencias ExactasQuímicaCalcium additionsolubilitysoybean protein isolatesResults of a study of the effect of calcium addition on polypeptide composition, hydrophobicity, sulfhydryl content, thermal stability, enthalpy of denaturation, and water solubility of soybean protein isolates suggest that the addition of small amounts of calcium (1.23–5.0 mg/g protein) induced the formation of α, α′ soluble aggregates, whereas large amounts (5.0–9.73 mg/g protein) induced the selective insolubilization of the glycinin fraction. The addition of this ion also produced thermal stabilization of the soybean proteins, mainly the glycinin fraction, and increased the enthalpy of denaturation. A decrease in the surface hydrophobicity of proteins with increasing calcium content was also observed. The results obtained suggested the existence of specific calcium-soy protein interactions, especially with the glycinin fraction.Centro de Investigación y Desarrollo en Criotecnología de Alimentos2004-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf63-69http://sedici.unlp.edu.ar/handle/10915/138658enginfo:eu-repo/semantics/altIdentifier/issn/0003-021xinfo:eu-repo/semantics/altIdentifier/issn/1558-9331info:eu-repo/semantics/altIdentifier/doi/10.1007/s11746-004-0858-yinfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/Creative Commons Attribution 4.0 International (CC BY 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:31:52Zoai:sedici.unlp.edu.ar:10915/138658Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:31:52.362SEDICI (UNLP) - Universidad Nacional de La Platafalse |
dc.title.none.fl_str_mv |
Characterization of soybean protein isolates : The effect of calcium presence |
title |
Characterization of soybean protein isolates : The effect of calcium presence |
spellingShingle |
Characterization of soybean protein isolates : The effect of calcium presence Scilingo, Adriana Alicia Ciencias Exactas Química Calcium addition solubility soybean protein isolates |
title_short |
Characterization of soybean protein isolates : The effect of calcium presence |
title_full |
Characterization of soybean protein isolates : The effect of calcium presence |
title_fullStr |
Characterization of soybean protein isolates : The effect of calcium presence |
title_full_unstemmed |
Characterization of soybean protein isolates : The effect of calcium presence |
title_sort |
Characterization of soybean protein isolates : The effect of calcium presence |
dc.creator.none.fl_str_mv |
Scilingo, Adriana Alicia Añón, María Cristina |
author |
Scilingo, Adriana Alicia |
author_facet |
Scilingo, Adriana Alicia Añón, María Cristina |
author_role |
author |
author2 |
Añón, María Cristina |
author2_role |
author |
dc.subject.none.fl_str_mv |
Ciencias Exactas Química Calcium addition solubility soybean protein isolates |
topic |
Ciencias Exactas Química Calcium addition solubility soybean protein isolates |
dc.description.none.fl_txt_mv |
Results of a study of the effect of calcium addition on polypeptide composition, hydrophobicity, sulfhydryl content, thermal stability, enthalpy of denaturation, and water solubility of soybean protein isolates suggest that the addition of small amounts of calcium (1.23–5.0 mg/g protein) induced the formation of α, α′ soluble aggregates, whereas large amounts (5.0–9.73 mg/g protein) induced the selective insolubilization of the glycinin fraction. The addition of this ion also produced thermal stabilization of the soybean proteins, mainly the glycinin fraction, and increased the enthalpy of denaturation. A decrease in the surface hydrophobicity of proteins with increasing calcium content was also observed. The results obtained suggested the existence of specific calcium-soy protein interactions, especially with the glycinin fraction. Centro de Investigación y Desarrollo en Criotecnología de Alimentos |
description |
Results of a study of the effect of calcium addition on polypeptide composition, hydrophobicity, sulfhydryl content, thermal stability, enthalpy of denaturation, and water solubility of soybean protein isolates suggest that the addition of small amounts of calcium (1.23–5.0 mg/g protein) induced the formation of α, α′ soluble aggregates, whereas large amounts (5.0–9.73 mg/g protein) induced the selective insolubilization of the glycinin fraction. The addition of this ion also produced thermal stabilization of the soybean proteins, mainly the glycinin fraction, and increased the enthalpy of denaturation. A decrease in the surface hydrophobicity of proteins with increasing calcium content was also observed. The results obtained suggested the existence of specific calcium-soy protein interactions, especially with the glycinin fraction. |
publishDate |
2004 |
dc.date.none.fl_str_mv |
2004-01-01 |
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/10915/138658 |
url |
http://sedici.unlp.edu.ar/handle/10915/138658 |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/issn/0003-021x info:eu-repo/semantics/altIdentifier/issn/1558-9331 info:eu-repo/semantics/altIdentifier/doi/10.1007/s11746-004-0858-y |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International (CC BY 4.0) |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International (CC BY 4.0) |
dc.format.none.fl_str_mv |
application/pdf 63-69 |
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Universidad Nacional de La Plata |
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SEDICI (UNLP) - Universidad Nacional de La Plata |
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alira@sedici.unlp.edu.ar |
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13.070432 |