Nonfreezing Water Structuration in Heteroprotein Coacervates
Surface-bound water in protein solutions has been identified with a reduction in its freezing point. We studied the presence of such nonfreezing water (NFW) in various protein-polyelectrolyte, micelle-polyelectrolyte, and protein-protein (heteroprotein) coacervates, along with appropriate concentrat...
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1992. - 31(2015), 31 vom: 11. Aug., Seite 8661-6 |
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| 1. Verfasser: | |
| Weitere Verfasser: | , , |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2015
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| Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Electrolytes Lactoglobulins Micelles Polymers Water 059QF0KO0R Serum Albumin, Bovine mehr... |
| Zusammenfassung: | Surface-bound water in protein solutions has been identified with a reduction in its freezing point. We studied the presence of such nonfreezing water (NFW) in various protein-polyelectrolyte, micelle-polyelectrolyte, and protein-protein (heteroprotein) coacervates, along with appropriate concentrated solutions of macromolecules alone, finding up to 15% w/w NFW for the heteroprotein coacervate of lactoferrin (LF) and β-lactoglobulin (BLG). The level of NFW is always higher in coacervates than in the control (single macromolecule) systems, particularly for protein-containing coacervates: a coacervate of bovine serum albumin (BSA) and poly(dimethyldiallylammonium chloride) (PDADMAC) showed a ratio of NFW/protein twice that of BSA alone (0.6 vs 0.3), with a similarly high ratio for LF-BLG coacervate. These results are attributed to the maximization of water-protein contacts, structural features that reflect the mode of sample assembly, as they are not seen in a noncoacervated LF-BLG solution with identical concentrations of all species |
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| Beschreibung: | Date Completed 26.04.2016 Date Revised 16.11.2017 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1520-5827 |
| DOI: | 10.1021/acs.langmuir.5b01647 |