Adsorption and rheological behavior of an amphiphilic protein at oil/water interfaces
- Hydrophobins are highly surface active proteins which self-assemble at hydrophilic-hydrophobic interfaces into amphipathic membranes. We investigate hydrophobin self-assembly at oil/water interfaces to deepen the understanding of protein behavior in order to improve our biomimetic synthesis. Therefore, we carried out pendant drop measurements of hydrophobin stabilized oil/water systems determining the time-dependent IFT and the dilatational rheology with additional adaptation to the Serrien protein model. We show that the class I hydrophobin H*Protein B adsorbs at an oil/water interface where it forms a densely-packed interfacial protein layer, which dissipates energy during droplet oscillation. Furthermore, the interfacial protein layer exhibits shear thinning behavior. (C) 2016 Elsevier Inc. All rights reserved.
| Verfasserangaben: | Marina Juliane Richter, Alexander Schulz, Thomas Subkowski, Alexander BökerORCiDGND |
|---|---|
| DOI: | https://doi.org/10.1016/j.jcis.2016.06.062 |
| ISSN: | 0021-9797 |
| ISSN: | 1095-7103 |
| Pubmed ID: | https://pubmed.ncbi.nlm.nih.gov/27388134 |
| Titel des übergeordneten Werks (Englisch): | Journal of colloid and interface science |
| Verlag: | Elsevier |
| Verlagsort: | San Diego |
| Publikationstyp: | Wissenschaftlicher Artikel |
| Sprache: | Englisch |
| Jahr der Erstveröffentlichung: | 2016 |
| Erscheinungsjahr: | 2016 |
| Datum der Freischaltung: | 22.03.2020 |
| Freies Schlagwort / Tag: | Hydrophobin; IFT; Pendant drop tensiometry; Rheology; Self-assembly |
| Band: | 479 |
| Seitenanzahl: | 8 |
| Erste Seite: | 199 |
| Letzte Seite: | 206 |
| Organisationseinheiten: | Mathematisch-Naturwissenschaftliche Fakultät / Institut für Chemie |
| Peer Review: | Referiert |
