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

Örnebro, J LU ; Wahlgren, M LU ; Eliasson, A-C LU ; Fido, R. J. and Tatham, A.S. (1999) In Journal of Cereal Science 77(5). p.105-114
Abstract (Swedish)
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.... (More)
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. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Cereal Science
volume
77
issue
5
pages
105 - 114
publisher
Elsevier
external identifiers
  • Scopus:0003950160
ISSN
0733-5210
DOI
10.1006/jcrs.1999.0270
language
English
LU publication?
yes
id
3b4b7d25-1632-440a-932c-58179bc8a537
date added to LUP
2016-04-15 19:28:07
date last changed
2017-02-02 08:59:36
@article{3b4b7d25-1632-440a-932c-58179bc8a537,
  abstract     = {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.},
  author       = {Örnebro, J and Wahlgren, M and Eliasson, A-C and Fido, R. J. and Tatham, A.S.},
  issn         = {0733-5210},
  language     = {eng},
  number       = {5},
  pages        = {105--114},
  publisher    = {Elsevier},
  series       = {Journal of Cereal Science},
  title        = {Adsorption of α-, β-, γ- and ω-Gliadins onto Hydrophobic Surfaces},
  url          = {http://dx.doi.org/10.1006/jcrs.1999.0270},
  volume       = {77},
  year         = {1999},
}