Adsorption of α-, β-, γ- and ω-Gliadins onto Hydrophobic Surfaces

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Adsorption onto hydrophobic surfaces of α-, β-, γ-, and ω-gliadins from the wheat variety Chinese Spring was studied by means of in situ ellipsometry. Most measurements were conducted in 0·01m phosphate buffer, pH 6·0, with the protein concentrations 1, 5 and 25 μg/mL. The adsorbed amount varied between 1·3 and 11·4 mg/m2, which is high considering the low protein concentrations. The concentration dependence was largest for the α-gliadins and lowest for the ω-gliadins. An intermediate concentration dependence was found for the β- and γ-gliadins, which also behaved similarly in all experiments. It was suggested that α-gliadins aggregated at the surface to a larger extent than the other gliadins when the protein concentration was 25 μg/mL. Further, it seemed as β- and γ-gliadins switched from a side-on orientation (major axis parallel to the surface) to an end-on orientation (major axis perpendicular to the surface) with increasing concentration, contrasting to the ω-gliadins that probably had side-on orientation at all concentrations. Sequential adsorption measurements indicated that α-, β-, and γ-gliadins blocked adsorption of ω-gliadins, but could replace ω-gliadins in a previously formed layer.


  • J Örnebro
  • M Wahlgren
  • A-C Eliasson
  • R. J. Fido
  • A.S. Tatham
External organisations
  • University of Bristol
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Food Science
Original languageEnglish
Pages (from-to)105-114
JournalJournal of Cereal Science
Issue number5
Publication statusPublished - 1999
Publication categoryResearch