The dynamics of heat gelation of casein glycomacropeptide - β-lactoglobulin mixtures as affected by interactions in the aqueous phase

The dynamics of heat gelation of casein glycomacropeptide (CMP) and β-lactoglobulin (β-lg) mixtures as affected by their interactions in the aqueous phase were studied at pH 3.5 and 7.0. At pH 7.0, whereas CMP did not gel, all the mixed systems gelled, but strong synergism was observed for 25:75 CMP...

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Autores principales: Martínez, María Julia, Farías, María Edith, Pilosof, Ana María Renata
Publicado: 2010
Materias:
Aqueous phase
DSC measurements
Electrostatically driven
Glycomacropeptide
Lactoglobulin
Mixed gel
Mixed systems
Casein
Coagulation
Gels
Gelation
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09586946_v20_n9_p580_Martinez
http://hdl.handle.net/20.500.12110/paper_09586946_v20_n9_p580_Martinez
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id paper:paper_09586946_v20_n9_p580_Martinez
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spelling paper:paper_09586946_v20_n9_p580_Martinez2025-07-30T18:32:52Z The dynamics of heat gelation of casein glycomacropeptide - β-lactoglobulin mixtures as affected by interactions in the aqueous phase Martínez, María Julia Farías, María Edith Pilosof, Ana María Renata Aqueous phase DSC measurements Electrostatically driven Glycomacropeptide Lactoglobulin Mixed gel Mixed systems Casein Coagulation Gels Gelation The dynamics of heat gelation of casein glycomacropeptide (CMP) and β-lactoglobulin (β-lg) mixtures as affected by their interactions in the aqueous phase were studied at pH 3.5 and 7.0. At pH 7.0, whereas CMP did not gel, all the mixed systems gelled, but strong synergism was observed for 25:75 CMP:β-lg ratio. In comparison, at pH 3.5 where both components gelled on their own, a strong antagonism was observed, mainly at 75:25 CMP:β-lg ratio. The behaviour of mixed gels is ascribed to the formation of electrostatically driven assembled CMP:β-lg structures, modulated by pH, which were observed by dynamic light scattering and DSC measurements. © 2009 Elsevier Ltd. Fil:Martinez, M.J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Farías, M.E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Pilosof, A.M.R. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2010 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09586946_v20_n9_p580_Martinez http://hdl.handle.net/20.500.12110/paper_09586946_v20_n9_p580_Martinez
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Aqueous phase
DSC measurements
Electrostatically driven
Glycomacropeptide
Lactoglobulin
Mixed gel
Mixed systems
Casein
Coagulation
Gels
Gelation
spellingShingle Aqueous phase
DSC measurements
Electrostatically driven
Glycomacropeptide
Lactoglobulin
Mixed gel
Mixed systems
Casein
Coagulation
Gels
Gelation
Martínez, María Julia
Farías, María Edith
Pilosof, Ana María Renata
The dynamics of heat gelation of casein glycomacropeptide - β-lactoglobulin mixtures as affected by interactions in the aqueous phase
topic_facet Aqueous phase
DSC measurements
Electrostatically driven
Glycomacropeptide
Lactoglobulin
Mixed gel
Mixed systems
Casein
Coagulation
Gels
Gelation
description The dynamics of heat gelation of casein glycomacropeptide (CMP) and β-lactoglobulin (β-lg) mixtures as affected by their interactions in the aqueous phase were studied at pH 3.5 and 7.0. At pH 7.0, whereas CMP did not gel, all the mixed systems gelled, but strong synergism was observed for 25:75 CMP:β-lg ratio. In comparison, at pH 3.5 where both components gelled on their own, a strong antagonism was observed, mainly at 75:25 CMP:β-lg ratio. The behaviour of mixed gels is ascribed to the formation of electrostatically driven assembled CMP:β-lg structures, modulated by pH, which were observed by dynamic light scattering and DSC measurements. © 2009 Elsevier Ltd.
author Martínez, María Julia
Farías, María Edith
Pilosof, Ana María Renata
author_facet Martínez, María Julia
Farías, María Edith
Pilosof, Ana María Renata
author_sort Martínez, María Julia
title The dynamics of heat gelation of casein glycomacropeptide - β-lactoglobulin mixtures as affected by interactions in the aqueous phase
title_short The dynamics of heat gelation of casein glycomacropeptide - β-lactoglobulin mixtures as affected by interactions in the aqueous phase
title_full The dynamics of heat gelation of casein glycomacropeptide - β-lactoglobulin mixtures as affected by interactions in the aqueous phase
title_fullStr The dynamics of heat gelation of casein glycomacropeptide - β-lactoglobulin mixtures as affected by interactions in the aqueous phase
title_full_unstemmed The dynamics of heat gelation of casein glycomacropeptide - β-lactoglobulin mixtures as affected by interactions in the aqueous phase
title_sort dynamics of heat gelation of casein glycomacropeptide - β-lactoglobulin mixtures as affected by interactions in the aqueous phase
publishDate 2010
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09586946_v20_n9_p580_Martinez
http://hdl.handle.net/20.500.12110/paper_09586946_v20_n9_p580_Martinez
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