Shear rheology of hydrophobic adsorption layers at oil/water interfaces and data interpretation in terms of a viscoelastic thixotropic model

G.M. Radulova, K.D. Danov, P.A. Kralchevsky, J.T. Petkov, S.D. Stoyanov

Research output: Contribution to journalArticleAcademicpeer-review

9 Citations (Scopus)

Abstract

Here, we investigate the surface shear rheology of class II HFBII hydrophobin layers at the oil/water interface. Experiments in two different dynamic regimes, at a fixed rate of strain and oscillations, have been carried out with a rotational rheometer. The rheological data obtained in both regimes comply with the same viscoelastic thixotropic model, which is used to determine the surface shear elasticity and viscosity, Esh and ¿sh. Their values for HFBII at oil/water interfaces are somewhat lower than those at the air/water interface. Moreover, Esh and ¿sh depend on the nature of oil, being smaller for hexadecane in comparison with soybean-oil. It is remarkable that Esh is independent of the rate of strain in the whole investigated range of shear rates. For oil/water interfaces, Esh and ¿sh determined for HFBII layers are considerably greater than for other proteins, like lysozyme and ß-casein. It is confirmed that the hydrophobin forms the most rigid surface layers among all investigated proteins not only for the air/water, but also for the oil/water interface. The wide applicability of the used viscoelastic thixotropic model is confirmed by analyzing data for adsorption layers at oil/water interfaces from lysozyme and ß-casein – both native and cross-linked by enzyme, as well as for films from asphaltene. This model turns out to be a versatile tool for determining the surface shear elasticity and viscosity, Esh and ¿sh, from experimental data for the surface storage and loss moduli, G' and G''.
Original languageEnglish
Pages (from-to)5777-5786
Number of pages9
JournalSoft Matter
Volume10
Issue number31
DOIs
Publication statusPublished - 2014

Keywords

  • oil-water interface
  • dependent relaxation-times
  • class-ii hydrophobin
  • protein hfbii
  • hexadecane/water interface
  • flexible proteins
  • bubble stability
  • beta-casein
  • surface
  • monolayers

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