@article{RichterSchulzSubkowskietal.2016,
  author    = {Richter, Marina Juliane and Schulz, Alexander and Subkowski, Thomas and B{\"o}ker, Alexander},
  title     = {Adsorption and rheological behavior of an amphiphilic protein at oil/water interfaces},
  series = {Journal of colloid and interface science},
  volume    = {479},
  journal   = {Journal of colloid and interface science},
  publisher = {Elsevier},
  address   = {San Diego},
  issn      = {0021-9797},
  doi       = {10.1016/j.jcis.2016.06.062},
  pages     = {199 -- 206},
  year      = {2016},
  abstract  = {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.},
  language  = {en}
}