Interactions between β-lactoglobulin and casein glycomacropeptide on foaming

The aim of this work was to study the effect of interactions between casein glycomacropeptide (CMP) and β-lactoglobulin (β-lg) at pH 6.5 and 3.5 on the foaming properties of the mixed systems with different CMP:β-lg ratios. The foaming properties were determined by the bubbling method with a Foamsca...

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Autores principales:	Martínez, María Julia, Pilosof, Ana María Renata
Publicado:	2012
Materias:	β-Lactoglobulin Casein glycomacropeptide Foam Interactions PH Aqueous phase Bubbling method Foaming properties Glycomacropeptide Lactoglobulin Mixed systems Differential scanning calorimetry Casein beta lactoglobulin casein glycoprotein adsorption article binding affinity chemical interaction complex formation concentration (parameters) controlled study density gradient differential scanning calorimetry down regulation foaming gelation light scattering mathematical model pH measurement priority journal protein protein interaction protein stability upregulation Caseins Glycopeptides Hydrogen-Ion Concentration Lactoglobulins Peptide Fragments
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09277765_v89_n1_p234_Martinez http://hdl.handle.net/20.500.12110/paper_09277765_v89_n1_p234_Martinez
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_09277765_v89_n1_p234_Martinez
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spelling	paper:paper_09277765_v89_n1_p234_Martinez2023-06-08T15:52:09Z Interactions between β-lactoglobulin and casein glycomacropeptide on foaming Martínez, María Julia Pilosof, Ana María Renata β-Lactoglobulin Casein glycomacropeptide Foam Interactions PH Aqueous phase Bubbling method Foaming properties Glycomacropeptide Lactoglobulin Mixed systems Differential scanning calorimetry Casein beta lactoglobulin casein glycoprotein adsorption article binding affinity chemical interaction complex formation concentration (parameters) controlled study density gradient differential scanning calorimetry down regulation foaming gelation light scattering mathematical model pH measurement priority journal protein protein interaction protein stability upregulation Caseins Glycopeptides Hydrogen-Ion Concentration Lactoglobulins Peptide Fragments The aim of this work was to study the effect of interactions between casein glycomacropeptide (CMP) and β-lactoglobulin (β-lg) at pH 6.5 and 3.5 on the foaming properties of the mixed systems with different CMP:β-lg ratios. The foaming properties were determined by the bubbling method with a Foamscan instrument. A highest overall foam capacity (OFC), foaming capacity (FC) and mainly stability of mixed foams at pH 3.5, as compared to the mixed foams at pH 6.5 or the foams of CMP and β-lg was observed. At pH 6.5, the stability of mixed foams decreased with increasing the CMP content, while OFC and FC values were similar to β-lg foam. The performance of the mixed systems was discussed in relation with the interactions between CMP and β-lg in the aqueous phase (as observed by dynamic light scattering and differential scanning calorimetry in previous works). © 2011 Elsevier B.V. Fil:Martinez, M.J. 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. 2012 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09277765_v89_n1_p234_Martinez http://hdl.handle.net/20.500.12110/paper_09277765_v89_n1_p234_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	β-Lactoglobulin Casein glycomacropeptide Foam Interactions PH Aqueous phase Bubbling method Foaming properties Glycomacropeptide Lactoglobulin Mixed systems Differential scanning calorimetry Casein beta lactoglobulin casein glycoprotein adsorption article binding affinity chemical interaction complex formation concentration (parameters) controlled study density gradient differential scanning calorimetry down regulation foaming gelation light scattering mathematical model pH measurement priority journal protein protein interaction protein stability upregulation Caseins Glycopeptides Hydrogen-Ion Concentration Lactoglobulins Peptide Fragments
spellingShingle	β-Lactoglobulin Casein glycomacropeptide Foam Interactions PH Aqueous phase Bubbling method Foaming properties Glycomacropeptide Lactoglobulin Mixed systems Differential scanning calorimetry Casein beta lactoglobulin casein glycoprotein adsorption article binding affinity chemical interaction complex formation concentration (parameters) controlled study density gradient differential scanning calorimetry down regulation foaming gelation light scattering mathematical model pH measurement priority journal protein protein interaction protein stability upregulation Caseins Glycopeptides Hydrogen-Ion Concentration Lactoglobulins Peptide Fragments Martínez, María Julia Pilosof, Ana María Renata Interactions between β-lactoglobulin and casein glycomacropeptide on foaming
topic_facet	β-Lactoglobulin Casein glycomacropeptide Foam Interactions PH Aqueous phase Bubbling method Foaming properties Glycomacropeptide Lactoglobulin Mixed systems Differential scanning calorimetry Casein beta lactoglobulin casein glycoprotein adsorption article binding affinity chemical interaction complex formation concentration (parameters) controlled study density gradient differential scanning calorimetry down regulation foaming gelation light scattering mathematical model pH measurement priority journal protein protein interaction protein stability upregulation Caseins Glycopeptides Hydrogen-Ion Concentration Lactoglobulins Peptide Fragments
description	The aim of this work was to study the effect of interactions between casein glycomacropeptide (CMP) and β-lactoglobulin (β-lg) at pH 6.5 and 3.5 on the foaming properties of the mixed systems with different CMP:β-lg ratios. The foaming properties were determined by the bubbling method with a Foamscan instrument. A highest overall foam capacity (OFC), foaming capacity (FC) and mainly stability of mixed foams at pH 3.5, as compared to the mixed foams at pH 6.5 or the foams of CMP and β-lg was observed. At pH 6.5, the stability of mixed foams decreased with increasing the CMP content, while OFC and FC values were similar to β-lg foam. The performance of the mixed systems was discussed in relation with the interactions between CMP and β-lg in the aqueous phase (as observed by dynamic light scattering and differential scanning calorimetry in previous works). © 2011 Elsevier B.V.
author	Martínez, María Julia Pilosof, Ana María Renata
author_facet	Martínez, María Julia Pilosof, Ana María Renata
author_sort	Martínez, María Julia
title	Interactions between β-lactoglobulin and casein glycomacropeptide on foaming
title_short	Interactions between β-lactoglobulin and casein glycomacropeptide on foaming
title_full	Interactions between β-lactoglobulin and casein glycomacropeptide on foaming
title_fullStr	Interactions between β-lactoglobulin and casein glycomacropeptide on foaming
title_full_unstemmed	Interactions between β-lactoglobulin and casein glycomacropeptide on foaming
title_sort	interactions between β-lactoglobulin and casein glycomacropeptide on foaming
publishDate	2012
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09277765_v89_n1_p234_Martinez http://hdl.handle.net/20.500.12110/paper_09277765_v89_n1_p234_Martinez
work_keys_str_mv	AT martinezmariajulia interactionsbetweenblactoglobulinandcaseinglycomacropeptideonfoaming AT pilosofanamariarenata interactionsbetweenblactoglobulinandcaseinglycomacropeptideonfoaming
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Interactions between β-lactoglobulin and casein glycomacropeptide on foaming

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