Modulating surface rheology by electrostatic protein/polysaccharide interactions

R.A. Ganzevles, K. Zinoviadou, T. van Vliet, M.A. Cohen Stuart, H.H.J. de Jongh

Research output: Contribution to journalArticleAcademicpeer-review

103 Citations (Scopus)


There is a large interest in mixed protein/polysaccharide layers at air-water and oil-water interfaces because of their ability to stabilize foams and emulsions. Mixed protein/polysaccharide adsorbed layers at air-water interfaces can be prepared either by adsorption of soluble protein/ polysaccharide complexes or by sequential adsorption of complexes or polysaccharides to a previously formed protein layer. Even though the final protein and polysaccharide bulk concentrations are the same, the behavior of the adsorbed layers can be very different, depending on the method of preparation. The surface shear modulus of a sequentially formed ß-lactoglobulin/pectin layer can be up to a factor of 6 higher than that of a layer made by simultaneous adsorption. Furthermore, the surface dilatational modulus and surface shear modulus strongly (up to factors of 2 and 7, respectively) depend on the bulk ß-lactoglobulin/pectin mixing ratio. On the basis of the surface rheological behavior, a mechanistic understanding of how the structure of the adsorbed layers depends on the protein/polysaccharide interaction in bulk solution, mixing ratio, ionic strength, and order of adsorption to the interface (simultaneous or sequential) is derived. Insight into the effect of protein/ polysaccharide interactions on the properties of adsorbed layers provides a solid basis to modulate surface rheological behavior
Original languageEnglish
Pages (from-to)10089-10096
Issue number24
Publication statusPublished - 2006


  • air-water-interface
  • adsorbed protein layers
  • beta-lactoglobulin
  • o/w emulsions
  • complex coacervation
  • air/water interface
  • foam stability
  • shear rheology
  • adsorption
  • pectin

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