On the crucial importance of the pH for the formation and self-stabilization of protein microgels and strands
© 2011 American Chemical Society
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1999. - 27(2011), 24 vom: 20. Dez., Seite 15092-101 |
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| 1. Verfasser: | |
| Weitere Verfasser: | , , , , |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2011
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| Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
| Schlagworte: | Journal Article Gels Lactoglobulins Salts Solutions |
| Zusammenfassung: | © 2011 American Chemical Society Stable suspensions of protein microgels are formed by heating salt-free β-lactoglobulin solutions at concentrations up to about C = 50 g·L(-1) if the pH is set within a narrow range between 5.75 and 6.1. The internal protein concentration of these spherical particles is about 150 g·L(-1) and the average hydrodynamic radius decreases with increasing pH from 200 to 75 nm. The formation of the microgels leads to an increase of the pH, which is a necessary condition to obtain stable suspensions. The spontaneous increase of the pH during microgel formation leads to an increase of their surface charge density and inhibits secondary aggregation. This self-stabilization mechanism is not sufficient if the initial pH is below 5.75 in which case secondary aggregation leads to precipitation. Microgels are no longer formed above a critical initial pH, but instead short, curved protein strands are obtained with a hydrodynamic radius of about 15-20 nm |
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| Beschreibung: | Date Completed 24.04.2012 Date Revised 14.12.2011 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1520-5827 |
| DOI: | 10.1021/la203357p |