Adsorption of α-, β-, γ- and ω-Gliadins onto Hydrophobic Surfaces
(1999) In Journal of Cereal Science 77(5). p.105-114- 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.... (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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https://lup.lub.lu.se/record/3b4b7d25-1632-440a-932c-58179bc8a537
- author
- Örnebro, J LU ; Wahlgren, M LU ; Eliasson, A-C LU ; Fido, R. J. and Tatham, A.S.
- organization
- publishing date
- 1999
- 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
- 2023-11-21 18:25:34
@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}}, doi = {{10.1006/jcrs.1999.0270}}, volume = {{77}}, year = {{1999}}, }