Casein glycomacropeptide pH-dependent self-assembly and cold gelation

Autores
Farias, M. E.; Martinez, María Julia; Pilosof, Ana Maria Renata
Año de publicación
2010
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The self-assembly of 3–5% (w/w) casein glycomacropeptide (CMP) at room temperature and pH 3–6.5 was determined by dynamic light scattering immediately after pH adjustment and over time, and the rate of gelation at a concentration of 3–10% (w/w) was determined by a tilting test. The intensity particle size distribution at pH 6.5 was multimodal with a predominant peak at 2.3 nm. The hydrodynamic diameter increased when decreasing the pH from 6.5 to 3. CMP solutions at a pH below 4.5 showed time-dependent self-assembly at room temperature, which led over time to gelation. The minimum concentration for cold gelation depended on pH. Below pH 4, CMP gelled even at low concentrations (3%, w/w). The pH-reversibility of self-assembled CMP was not total, showing that hydrophobically bound dimers, once formed, are stable to pH changes. A model to explain CMP self-assembly and the formation of a network-like structure (gel) at room temperature is proposed.
Fil: Farias, M. E.. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina. Universidad Nacional de Luján. Departamento de Tecnología; Argentina
Fil: Martinez, María Julia. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Pilosof, Ana Maria Renata. Universidad Nacional de Luján. Departamento de Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Materia
Casein Glycomacropeptide
Self-Assembly
Gelation
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/16363
Acceder
id CONICETDig_77128ce8d3e6615d6e3b03cfa877337c
oai_identifier_str oai:ri.conicet.gov.ar:11336/16363
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Casein glycomacropeptide pH-dependent self-assembly and cold gelationFarias, M. E.Martinez, María JuliaPilosof, Ana Maria RenataCasein GlycomacropeptideSelf-AssemblyGelationhttps://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2The self-assembly of 3–5% (w/w) casein glycomacropeptide (CMP) at room temperature and pH 3–6.5 was determined by dynamic light scattering immediately after pH adjustment and over time, and the rate of gelation at a concentration of 3–10% (w/w) was determined by a tilting test. The intensity particle size distribution at pH 6.5 was multimodal with a predominant peak at 2.3 nm. The hydrodynamic diameter increased when decreasing the pH from 6.5 to 3. CMP solutions at a pH below 4.5 showed time-dependent self-assembly at room temperature, which led over time to gelation. The minimum concentration for cold gelation depended on pH. Below pH 4, CMP gelled even at low concentrations (3%, w/w). The pH-reversibility of self-assembled CMP was not total, showing that hydrophobically bound dimers, once formed, are stable to pH changes. A model to explain CMP self-assembly and the formation of a network-like structure (gel) at room temperature is proposed.Fil: Farias, M. E.. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina. Universidad Nacional de Luján. Departamento de Tecnología; ArgentinaFil: Martinez, María Julia. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Pilosof, Ana Maria Renata. Universidad Nacional de Luján. Departamento de Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaElsevier2010-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/16363Farias, M. E.; Martinez, María Julia; Pilosof, Ana Maria Renata; Casein glycomacropeptide pH-dependent self-assembly and cold gelation; Elsevier; International Dairy Journal; 20; 2; 2-2010; 79-880958-6946enginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.idairyj.2009.09.002info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0958694609001691info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:23:44Zoai:ri.conicet.gov.ar:11336/16363instacron: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:34982025-09-29 10:23:44.396CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Casein glycomacropeptide pH-dependent self-assembly and cold gelation
title Casein glycomacropeptide pH-dependent self-assembly and cold gelation
spellingShingle Casein glycomacropeptide pH-dependent self-assembly and cold gelation
Farias, M. E.
Casein Glycomacropeptide
Self-Assembly
Gelation
title_short Casein glycomacropeptide pH-dependent self-assembly and cold gelation
title_full Casein glycomacropeptide pH-dependent self-assembly and cold gelation
title_fullStr Casein glycomacropeptide pH-dependent self-assembly and cold gelation
title_full_unstemmed Casein glycomacropeptide pH-dependent self-assembly and cold gelation
title_sort Casein glycomacropeptide pH-dependent self-assembly and cold gelation
dc.creator.none.fl_str_mv Farias, M. E.
Martinez, María Julia
Pilosof, Ana Maria Renata
author Farias, M. E.
author_facet Farias, M. E.
Martinez, María Julia
Pilosof, Ana Maria Renata
author_role author
author2 Martinez, María Julia
Pilosof, Ana Maria Renata
author2_role author
author
dc.subject.none.fl_str_mv Casein Glycomacropeptide
Self-Assembly
Gelation
topic Casein Glycomacropeptide
Self-Assembly
Gelation
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.11
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv The self-assembly of 3–5% (w/w) casein glycomacropeptide (CMP) at room temperature and pH 3–6.5 was determined by dynamic light scattering immediately after pH adjustment and over time, and the rate of gelation at a concentration of 3–10% (w/w) was determined by a tilting test. The intensity particle size distribution at pH 6.5 was multimodal with a predominant peak at 2.3 nm. The hydrodynamic diameter increased when decreasing the pH from 6.5 to 3. CMP solutions at a pH below 4.5 showed time-dependent self-assembly at room temperature, which led over time to gelation. The minimum concentration for cold gelation depended on pH. Below pH 4, CMP gelled even at low concentrations (3%, w/w). The pH-reversibility of self-assembled CMP was not total, showing that hydrophobically bound dimers, once formed, are stable to pH changes. A model to explain CMP self-assembly and the formation of a network-like structure (gel) at room temperature is proposed.
Fil: Farias, M. E.. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina. Universidad Nacional de Luján. Departamento de Tecnología; Argentina
Fil: Martinez, María Julia. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Pilosof, Ana Maria Renata. Universidad Nacional de Luján. Departamento de Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
description The self-assembly of 3–5% (w/w) casein glycomacropeptide (CMP) at room temperature and pH 3–6.5 was determined by dynamic light scattering immediately after pH adjustment and over time, and the rate of gelation at a concentration of 3–10% (w/w) was determined by a tilting test. The intensity particle size distribution at pH 6.5 was multimodal with a predominant peak at 2.3 nm. The hydrodynamic diameter increased when decreasing the pH from 6.5 to 3. CMP solutions at a pH below 4.5 showed time-dependent self-assembly at room temperature, which led over time to gelation. The minimum concentration for cold gelation depended on pH. Below pH 4, CMP gelled even at low concentrations (3%, w/w). The pH-reversibility of self-assembled CMP was not total, showing that hydrophobically bound dimers, once formed, are stable to pH changes. A model to explain CMP self-assembly and the formation of a network-like structure (gel) at room temperature is proposed.
publishDate 2010
dc.date.none.fl_str_mv 2010-02
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/11336/16363
Farias, M. E.; Martinez, María Julia; Pilosof, Ana Maria Renata; Casein glycomacropeptide pH-dependent self-assembly and cold gelation; Elsevier; International Dairy Journal; 20; 2; 2-2010; 79-88
0958-6946
url http://hdl.handle.net/11336/16363
identifier_str_mv Farias, M. E.; Martinez, María Julia; Pilosof, Ana Maria Renata; Casein glycomacropeptide pH-dependent self-assembly and cold gelation; Elsevier; International Dairy Journal; 20; 2; 2-2010; 79-88
0958-6946
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.idairyj.2009.09.002
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0958694609001691
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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
_version_ 1844614233049792512
score 13.070432

Publicaciones similares