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Adsorption and rheological behavior of an amphiphilic protein at oil/water interfaces

: Richter, M.J.; Schulz, A.; Subkowski, T.; Böker, A.


Journal of colloid and interface science 479 (2016), pp.199-206
ISSN: 0021-9797
Journal Article
Fraunhofer IAP ()

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 HâProtein 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.