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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.
| Author details: | 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 |
| Title of parent work (English): | Journal of colloid and interface science |
| Publisher: | Elsevier |
| Place of publishing: | San Diego |
| Publication type: | Article |
| Language: | English |
| Year of first publication: | 2016 |
| Publication year: | 2016 |
| Release date: | 2020/03/22 |
| Tag: | Hydrophobin; IFT; Pendant drop tensiometry; Rheology; Self-assembly |
| Volume: | 479 |
| Number of pages: | 8 |
| First page: | 199 |
| Last Page: | 206 |
| Organizational units: | Mathematisch-Naturwissenschaftliche Fakultät / Institut für Chemie |
| Peer review: | Referiert |
