Casein glycomacropeptide pH-dependent self-assembly and cold gelation
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 particl...
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2010
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09586946_v20_n2_p79_Farias http://hdl.handle.net/20.500.12110/paper_09586946_v20_n2_p79_Farias |
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paper:paper_09586946_v20_n2_p79_Farias2023-06-08T15:56:42Z Casein glycomacropeptide pH-dependent self-assembly and cold gelation Farías, María Edith Martínez, María Julia Pilosof, Ana María Renata Concentration of Glycomacropeptide Hydrodynamic diameter Low concentrations Multi-modal PH adjustment pH change PH-dependent Room temperature Self-assembled Time-dependent Casein Coagulation Fluid dynamics Gelation Oligomers Self assembly Nanotechnology 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. © 2009 Elsevier Ltd. All rights reserved. Fil:Farías, M.E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 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. 2010 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09586946_v20_n2_p79_Farias http://hdl.handle.net/20.500.12110/paper_09586946_v20_n2_p79_Farias |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Concentration of Glycomacropeptide Hydrodynamic diameter Low concentrations Multi-modal PH adjustment pH change PH-dependent Room temperature Self-assembled Time-dependent Casein Coagulation Fluid dynamics Gelation Oligomers Self assembly Nanotechnology |
| spellingShingle |
Concentration of Glycomacropeptide Hydrodynamic diameter Low concentrations Multi-modal PH adjustment pH change PH-dependent Room temperature Self-assembled Time-dependent Casein Coagulation Fluid dynamics Gelation Oligomers Self assembly Nanotechnology Farías, María Edith Martínez, María Julia Pilosof, Ana María Renata Casein glycomacropeptide pH-dependent self-assembly and cold gelation |
| topic_facet |
Concentration of Glycomacropeptide Hydrodynamic diameter Low concentrations Multi-modal PH adjustment pH change PH-dependent Room temperature Self-assembled Time-dependent Casein Coagulation Fluid dynamics Gelation Oligomers Self assembly Nanotechnology |
| 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. © 2009 Elsevier Ltd. All rights reserved. |
| author |
Farías, María Edith Martínez, María Julia Pilosof, Ana María Renata |
| author_facet |
Farías, María Edith Martínez, María Julia Pilosof, Ana María Renata |
| author_sort |
Farías, María Edith |
| title |
Casein glycomacropeptide pH-dependent self-assembly and cold 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 |
| publishDate |
2010 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09586946_v20_n2_p79_Farias http://hdl.handle.net/20.500.12110/paper_09586946_v20_n2_p79_Farias |
| work_keys_str_mv |
AT fariasmariaedith caseinglycomacropeptidephdependentselfassemblyandcoldgelation AT martinezmariajulia caseinglycomacropeptidephdependentselfassemblyandcoldgelation AT pilosofanamariarenata caseinglycomacropeptidephdependentselfassemblyandcoldgelation |
| _version_ |
1768546261608169472 |