Bulk and interfacial behaviour of caseinoglycomacropeptide (GMP)
Caseinoglycomacropeptide (GMP) is a hydrophilic glycopeptide released from milk κ-casein by chymosin hydrolysis during cheese making. GMP is thought to be a potential ingredient for specific dietary applications with several health benefits. In this study GMP was characterized at the air-water inter...
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todo:paper_09277765_v71_n2_p230_Martinez2023-10-03T15:47:15Z Bulk and interfacial behaviour of caseinoglycomacropeptide (GMP) Martinez, M.J. Sánchez, C.C. Patino, J.M.R. Pilosof, A.M.R. Caseinoglycomacropeptide Dynamic light scattering Interface pH Air-water interfaces Bulk concentrations Caseinoglycomacropeptide Cheese makings Chymosin Dynamic measurements Electrostatic interactions Glycopeptide Health benefits Interface Interfacial properties Protein-protein interactions Self- assemblies Surface pressures Tensiometry Visco-elastic properties Adsorption Air Dynamic light scattering Rate constants Refraction Scattering Self assembly Phase interfaces caseinoglycomacropeptide chymosin glycopeptide kappa casein peptide derivative protein unclassified drug water adsorption air article bulk density cheesemaking concentration (parameters) diffusion dynamic exercise dynamics electricity equilibrium constant hydrolysis hydrophilicity light scattering measurement milk nutritional assessment pH pressure priority journal protein interaction stereospecificity viscoelasticity Adsorption Air Caseins Diffusion Elasticity Glycopeptides Hydrogen-Ion Concentration Kinetics Milk Proteins Particle Size Pressure Solutions Surface Properties Temperature Time Factors Viscoelastic Substances Viscosity Water Caseinoglycomacropeptide (GMP) is a hydrophilic glycopeptide released from milk κ-casein by chymosin hydrolysis during cheese making. GMP is thought to be a potential ingredient for specific dietary applications with several health benefits. In this study GMP was characterized at the air-water interface and its behaviour was related with the self-assembly of GMP in solution as affected by pH. This GMP self-assembly was investigated by dynamic light scattering and the interfacial properties were determined by tensiometry and surface dilatational measurements at pH 4, 5 and 7. At pH 5 GMP exhibited higher surface pressure at equilibrium than at pH 7. At pH 4 the behaviour was more complex due to self-assembly close to GMP pI. Dynamic measurement showed that the adsorption/penetration rate constant (Kads) is facilitated at higher GMP bulk concentrations, while the rate constant of rearrangement (Kr) decreased at higher GMP concentrations which could be attributed to the existence of a steric restriction due to the higher GMP load at the interface. Kr was higher at pH 5 because of lower electrostatic interactions close to the pI. The viscoelastic properties showed a complex behaviour due to the existence of protein-protein interactions depending on the GMP concentration, on the pH of the bulk and on the rates of diffusion, adsorption and rearrangement of GMP at the air-water interface. © 2009 Elsevier B.V. All rights reserved. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_09277765_v71_n2_p230_Martinez |
| institution |
Universidad de Buenos Aires |
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I-28 |
| repository_str |
R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Caseinoglycomacropeptide Dynamic light scattering Interface pH Air-water interfaces Bulk concentrations Caseinoglycomacropeptide Cheese makings Chymosin Dynamic measurements Electrostatic interactions Glycopeptide Health benefits Interface Interfacial properties Protein-protein interactions Self- assemblies Surface pressures Tensiometry Visco-elastic properties Adsorption Air Dynamic light scattering Rate constants Refraction Scattering Self assembly Phase interfaces caseinoglycomacropeptide chymosin glycopeptide kappa casein peptide derivative protein unclassified drug water adsorption air article bulk density cheesemaking concentration (parameters) diffusion dynamic exercise dynamics electricity equilibrium constant hydrolysis hydrophilicity light scattering measurement milk nutritional assessment pH pressure priority journal protein interaction stereospecificity viscoelasticity Adsorption Air Caseins Diffusion Elasticity Glycopeptides Hydrogen-Ion Concentration Kinetics Milk Proteins Particle Size Pressure Solutions Surface Properties Temperature Time Factors Viscoelastic Substances Viscosity Water |
| spellingShingle |
Caseinoglycomacropeptide Dynamic light scattering Interface pH Air-water interfaces Bulk concentrations Caseinoglycomacropeptide Cheese makings Chymosin Dynamic measurements Electrostatic interactions Glycopeptide Health benefits Interface Interfacial properties Protein-protein interactions Self- assemblies Surface pressures Tensiometry Visco-elastic properties Adsorption Air Dynamic light scattering Rate constants Refraction Scattering Self assembly Phase interfaces caseinoglycomacropeptide chymosin glycopeptide kappa casein peptide derivative protein unclassified drug water adsorption air article bulk density cheesemaking concentration (parameters) diffusion dynamic exercise dynamics electricity equilibrium constant hydrolysis hydrophilicity light scattering measurement milk nutritional assessment pH pressure priority journal protein interaction stereospecificity viscoelasticity Adsorption Air Caseins Diffusion Elasticity Glycopeptides Hydrogen-Ion Concentration Kinetics Milk Proteins Particle Size Pressure Solutions Surface Properties Temperature Time Factors Viscoelastic Substances Viscosity Water Martinez, M.J. Sánchez, C.C. Patino, J.M.R. Pilosof, A.M.R. Bulk and interfacial behaviour of caseinoglycomacropeptide (GMP) |
| topic_facet |
Caseinoglycomacropeptide Dynamic light scattering Interface pH Air-water interfaces Bulk concentrations Caseinoglycomacropeptide Cheese makings Chymosin Dynamic measurements Electrostatic interactions Glycopeptide Health benefits Interface Interfacial properties Protein-protein interactions Self- assemblies Surface pressures Tensiometry Visco-elastic properties Adsorption Air Dynamic light scattering Rate constants Refraction Scattering Self assembly Phase interfaces caseinoglycomacropeptide chymosin glycopeptide kappa casein peptide derivative protein unclassified drug water adsorption air article bulk density cheesemaking concentration (parameters) diffusion dynamic exercise dynamics electricity equilibrium constant hydrolysis hydrophilicity light scattering measurement milk nutritional assessment pH pressure priority journal protein interaction stereospecificity viscoelasticity Adsorption Air Caseins Diffusion Elasticity Glycopeptides Hydrogen-Ion Concentration Kinetics Milk Proteins Particle Size Pressure Solutions Surface Properties Temperature Time Factors Viscoelastic Substances Viscosity Water |
| description |
Caseinoglycomacropeptide (GMP) is a hydrophilic glycopeptide released from milk κ-casein by chymosin hydrolysis during cheese making. GMP is thought to be a potential ingredient for specific dietary applications with several health benefits. In this study GMP was characterized at the air-water interface and its behaviour was related with the self-assembly of GMP in solution as affected by pH. This GMP self-assembly was investigated by dynamic light scattering and the interfacial properties were determined by tensiometry and surface dilatational measurements at pH 4, 5 and 7. At pH 5 GMP exhibited higher surface pressure at equilibrium than at pH 7. At pH 4 the behaviour was more complex due to self-assembly close to GMP pI. Dynamic measurement showed that the adsorption/penetration rate constant (Kads) is facilitated at higher GMP bulk concentrations, while the rate constant of rearrangement (Kr) decreased at higher GMP concentrations which could be attributed to the existence of a steric restriction due to the higher GMP load at the interface. Kr was higher at pH 5 because of lower electrostatic interactions close to the pI. The viscoelastic properties showed a complex behaviour due to the existence of protein-protein interactions depending on the GMP concentration, on the pH of the bulk and on the rates of diffusion, adsorption and rearrangement of GMP at the air-water interface. © 2009 Elsevier B.V. All rights reserved. |
| format |
JOUR |
| author |
Martinez, M.J. Sánchez, C.C. Patino, J.M.R. Pilosof, A.M.R. |
| author_facet |
Martinez, M.J. Sánchez, C.C. Patino, J.M.R. Pilosof, A.M.R. |
| author_sort |
Martinez, M.J. |
| title |
Bulk and interfacial behaviour of caseinoglycomacropeptide (GMP) |
| title_short |
Bulk and interfacial behaviour of caseinoglycomacropeptide (GMP) |
| title_full |
Bulk and interfacial behaviour of caseinoglycomacropeptide (GMP) |
| title_fullStr |
Bulk and interfacial behaviour of caseinoglycomacropeptide (GMP) |
| title_full_unstemmed |
Bulk and interfacial behaviour of caseinoglycomacropeptide (GMP) |
| title_sort |
bulk and interfacial behaviour of caseinoglycomacropeptide (gmp) |
| url |
http://hdl.handle.net/20.500.12110/paper_09277765_v71_n2_p230_Martinez |
| work_keys_str_mv |
AT martinezmj bulkandinterfacialbehaviourofcaseinoglycomacropeptidegmp AT sanchezcc bulkandinterfacialbehaviourofcaseinoglycomacropeptidegmp AT patinojmr bulkandinterfacialbehaviourofcaseinoglycomacropeptidegmp AT pilosofamr bulkandinterfacialbehaviourofcaseinoglycomacropeptidegmp |
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