Shear rheology of mixed protein adsorption layers vs their structure studied by surface force measurements

K.D. Danov, P.A. Kralchevsky, G.M. Radulova, E.S. Basheva, S.D. Stoyanov, E.G. Pelan

Research output: Contribution to journalArticleAcademicpeer-review

16 Citations (Scopus)


The hydrophobins are proteins that form the most rigid adsorption layers at liquid interfaces in comparison with all other investigated proteins. The mixing of hydrophobin HFBII with other conventional proteins is expected to reduce the surface shear elasticity and viscosity, Esh and ¿sh, proportional to the fraction of the conventional protein. However, the experiments show that the effect of mixing can be rather different depending on the nature of the additive. If the additive is a globular protein, like ß-lactoglobulin and ovalbumin, the surface rigidity is preserved, and even enhanced. The experiments with separate foam films indicate that this is due to the formation of a bilayer structure at the air/water interface. The more hydrophobic HFBII forms the upper layer adjacent to the air phase, whereas the conventional globular protein forms the lower layer that faces the water phase. Thus, the elastic network formed by the adsorbed hydrophobin remains intact, and even reinforced by the adjacent layer of globular protein. In contrast, the addition of the disordered protein ß-casein leads to softening of the HFBII adsorption layer. Similar (an even stronger) effect is produced by the nonionic surfactant Tween 20. This can be explained with the penetration of the hydrophobic tails of ß-casein and Tween 20 between the HFBII molecules at the interface, which breaks the integrity of the hydrophobin interfacial elastic network. The analyzed experimental data for the surface shear rheology of various protein adsorption layers comply with a viscoelastic thixotropic model, which allows one to determine Esh and ¿sh from the measured storage and loss moduli, G' and G¿. The results could contribute for quantitative characterization and deeper understanding of the factors that control the surface rigidity of protein adsorption layers with potential application for the creation of stable foams and emulsions with fine bubbles or droplets.
Original languageEnglish
Pages (from-to)148-161
JournalAdvances in Colloid and Interface Science
Publication statusPublished - 2015


  • nonlinear viscoelastic model
  • dependent relaxation-times
  • class-ii hydrophobin
  • low ionic-strength
  • beta-casein
  • interfacial rheology
  • air/water interface
  • liquid interfaces
  • bubble stability
  • hfbii

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