Relation between solubility and surface hydrophobicity as an indicator of modifications during preparation processes of commercial and laboratory prepared soy protein isolates

Autores
Wagner, Jorge Ricardo; Sorgentini, Delia A.; Añon, Maria Cristina
Año de publicación
2000
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Because water solubility is the main hydration property of proteins, solubility values of commercial and laboratory soy protein isolates, prepared under different conditions, were comparatively analyzed. In contrast, the surface hydrophobicity manifested by proteins is a physicochemical property that determines, to a great extent, the tendency of protein molecules to aggregate and so to lose solubility. On these grounds, the solubility of isolates was analyzed as a function of the surface hydrophobicity of their proteins, and, as a result, three well-defined groups of laboratory isolates were identified: (A) native, (B) partially or totally denatured with high solubility and surface hydrophobicity, and (C) totally denatured with low solubility and surface hydrophobicity. Commercial isolates could not be included in any of these groups; they were grouped as (A') partially native and (C') totally denatured. Solubility values in these two groups were similar to those of group C, but the surface hydrophobicity levels were much lower. The different processes leading to the groups mentioned above are discussed, along with the way the soy proteins are influenced by the specific preparation conditions, namely, protein concentration, chemical or thermal treatments, presence of salts, drying, and phospholipid addition, among others.
Fil: Wagner, Jorge Ricardo. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina
Fil: Sorgentini, Delia A.. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas; Argentina
Fil: Añon, Maria Cristina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina
Materia
Modified Isolates
Solubility
Soy Isolates
Soy Proteins
Surface Hydrophobicity
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:11336/71762
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/71762
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repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Relation between solubility and surface hydrophobicity as an indicator of modifications during preparation processes of commercial and laboratory prepared soy protein isolatesWagner, Jorge RicardoSorgentini, Delia A.Añon, Maria CristinaModified IsolatesSolubilitySoy IsolatesSoy ProteinsSurface Hydrophobicityhttps://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2Because water solubility is the main hydration property of proteins, solubility values of commercial and laboratory soy protein isolates, prepared under different conditions, were comparatively analyzed. In contrast, the surface hydrophobicity manifested by proteins is a physicochemical property that determines, to a great extent, the tendency of protein molecules to aggregate and so to lose solubility. On these grounds, the solubility of isolates was analyzed as a function of the surface hydrophobicity of their proteins, and, as a result, three well-defined groups of laboratory isolates were identified: (A) native, (B) partially or totally denatured with high solubility and surface hydrophobicity, and (C) totally denatured with low solubility and surface hydrophobicity. Commercial isolates could not be included in any of these groups; they were grouped as (A') partially native and (C') totally denatured. Solubility values in these two groups were similar to those of group C, but the surface hydrophobicity levels were much lower. The different processes leading to the groups mentioned above are discussed, along with the way the soy proteins are influenced by the specific preparation conditions, namely, protein concentration, chemical or thermal treatments, presence of salts, drying, and phospholipid addition, among others.Fil: Wagner, Jorge Ricardo. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; ArgentinaFil: Sorgentini, Delia A.. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas; ArgentinaFil: Añon, Maria Cristina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; ArgentinaAmerican Chemical Society2000-06info: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/11336/71762Wagner, Jorge Ricardo; Sorgentini, Delia A.; Añon, Maria Cristina; Relation between solubility and surface hydrophobicity as an indicator of modifications during preparation processes of commercial and laboratory prepared soy protein isolates; American Chemical Society; Journal of Agricultural and Food Chemistry; 48; 8; 6-2000; 3159-31650021-8561CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/abs/10.1021/jf990823binfo:eu-repo/semantics/altIdentifier/doi/10.1021/jf990823binfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-10T13:06:44Zoai:ri.conicet.gov.ar:11336/71762instacron: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:34982025-09-10 13:06:44.631CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Relation between solubility and surface hydrophobicity as an indicator of modifications during preparation processes of commercial and laboratory prepared soy protein isolates
title Relation between solubility and surface hydrophobicity as an indicator of modifications during preparation processes of commercial and laboratory prepared soy protein isolates
spellingShingle Relation between solubility and surface hydrophobicity as an indicator of modifications during preparation processes of commercial and laboratory prepared soy protein isolates
Wagner, Jorge Ricardo
Modified Isolates
Solubility
Soy Isolates
Soy Proteins
Surface Hydrophobicity
title_short Relation between solubility and surface hydrophobicity as an indicator of modifications during preparation processes of commercial and laboratory prepared soy protein isolates
title_full Relation between solubility and surface hydrophobicity as an indicator of modifications during preparation processes of commercial and laboratory prepared soy protein isolates
title_fullStr Relation between solubility and surface hydrophobicity as an indicator of modifications during preparation processes of commercial and laboratory prepared soy protein isolates
title_full_unstemmed Relation between solubility and surface hydrophobicity as an indicator of modifications during preparation processes of commercial and laboratory prepared soy protein isolates
title_sort Relation between solubility and surface hydrophobicity as an indicator of modifications during preparation processes of commercial and laboratory prepared soy protein isolates
dc.creator.none.fl_str_mv Wagner, Jorge Ricardo
Sorgentini, Delia A.
Añon, Maria Cristina
author Wagner, Jorge Ricardo
author_facet Wagner, Jorge Ricardo
Sorgentini, Delia A.
Añon, Maria Cristina
author_role author
author2 Sorgentini, Delia A.
Añon, Maria Cristina
author2_role author
author
dc.subject.none.fl_str_mv Modified Isolates
Solubility
Soy Isolates
Soy Proteins
Surface Hydrophobicity
topic Modified Isolates
Solubility
Soy Isolates
Soy Proteins
Surface Hydrophobicity
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.11
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv Because water solubility is the main hydration property of proteins, solubility values of commercial and laboratory soy protein isolates, prepared under different conditions, were comparatively analyzed. In contrast, the surface hydrophobicity manifested by proteins is a physicochemical property that determines, to a great extent, the tendency of protein molecules to aggregate and so to lose solubility. On these grounds, the solubility of isolates was analyzed as a function of the surface hydrophobicity of their proteins, and, as a result, three well-defined groups of laboratory isolates were identified: (A) native, (B) partially or totally denatured with high solubility and surface hydrophobicity, and (C) totally denatured with low solubility and surface hydrophobicity. Commercial isolates could not be included in any of these groups; they were grouped as (A') partially native and (C') totally denatured. Solubility values in these two groups were similar to those of group C, but the surface hydrophobicity levels were much lower. The different processes leading to the groups mentioned above are discussed, along with the way the soy proteins are influenced by the specific preparation conditions, namely, protein concentration, chemical or thermal treatments, presence of salts, drying, and phospholipid addition, among others.
Fil: Wagner, Jorge Ricardo. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina
Fil: Sorgentini, Delia A.. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas; Argentina
Fil: Añon, Maria Cristina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina
description Because water solubility is the main hydration property of proteins, solubility values of commercial and laboratory soy protein isolates, prepared under different conditions, were comparatively analyzed. In contrast, the surface hydrophobicity manifested by proteins is a physicochemical property that determines, to a great extent, the tendency of protein molecules to aggregate and so to lose solubility. On these grounds, the solubility of isolates was analyzed as a function of the surface hydrophobicity of their proteins, and, as a result, three well-defined groups of laboratory isolates were identified: (A) native, (B) partially or totally denatured with high solubility and surface hydrophobicity, and (C) totally denatured with low solubility and surface hydrophobicity. Commercial isolates could not be included in any of these groups; they were grouped as (A') partially native and (C') totally denatured. Solubility values in these two groups were similar to those of group C, but the surface hydrophobicity levels were much lower. The different processes leading to the groups mentioned above are discussed, along with the way the soy proteins are influenced by the specific preparation conditions, namely, protein concentration, chemical or thermal treatments, presence of salts, drying, and phospholipid addition, among others.
publishDate 2000
dc.date.none.fl_str_mv 2000-06
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/11336/71762
Wagner, Jorge Ricardo; Sorgentini, Delia A.; Añon, Maria Cristina; Relation between solubility and surface hydrophobicity as an indicator of modifications during preparation processes of commercial and laboratory prepared soy protein isolates; American Chemical Society; Journal of Agricultural and Food Chemistry; 48; 8; 6-2000; 3159-3165
0021-8561
CONICET Digital
CONICET
url http://hdl.handle.net/11336/71762
identifier_str_mv Wagner, Jorge Ricardo; Sorgentini, Delia A.; Añon, Maria Cristina; Relation between solubility and surface hydrophobicity as an indicator of modifications during preparation processes of commercial and laboratory prepared soy protein isolates; American Chemical Society; Journal of Agricultural and Food Chemistry; 48; 8; 6-2000; 3159-3165
0021-8561
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/abs/10.1021/jf990823b
info:eu-repo/semantics/altIdentifier/doi/10.1021/jf990823b
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 12.993085

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