The behaviour of the high molecular-weight glutenin subunit 1Dx5, the 58 kDa central repetitive domain and a-gliadins at the air-aqueous interface.
(2003) In Journal of Cereal Science 38(2). p.147-156- Abstract
- The surface pressure–molecular area (–A) relationship for spread layers of the high molecular-weight glutenin subunit 1Dx5, a 58 kDa peptide derived from the central repetitive domain of the subunit, and an -gliadin fraction was measured by means of a surface film balance (Langmuir trough). The aqueous phase was a 10 mM acetate buffer, pH 4.0, either with or without 100 mM NaCl. Subunit 1Dx5 generated much higher surface pressures than the 58 kDa peptide, whereas the -gliadin fraction generally gave higher surface pressures than subunit 1Dx5. Furthermore, subunit 1Dx5, but not the 58 kDa peptide or the -gliadin fraction, formed a highly cohesive film. The differences in the interfacial behaviour of subunit 1Dx5 and the 58 kDa peptide were... (More)
- The surface pressure–molecular area (–A) relationship for spread layers of the high molecular-weight glutenin subunit 1Dx5, a 58 kDa peptide derived from the central repetitive domain of the subunit, and an -gliadin fraction was measured by means of a surface film balance (Langmuir trough). The aqueous phase was a 10 mM acetate buffer, pH 4.0, either with or without 100 mM NaCl. Subunit 1Dx5 generated much higher surface pressures than the 58 kDa peptide, whereas the -gliadin fraction generally gave higher surface pressures than subunit 1Dx5. Furthermore, subunit 1Dx5, but not the 58 kDa peptide or the -gliadin fraction, formed a highly cohesive film. The differences in the interfacial behaviour of subunit 1Dx5 and the 58 kDa peptide were ascribed to significant hydrophobic interactions for the subunit. The reversibility of a compression–expansion cycle was generally greater for the second cycle than for the first. For subunit 1Dx5 and the -gliadins, but not the 58 kDa peptide, the reversibility was increased when NaCl was present in the aqueous phase. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/128307
- author
- Örnebro, Jörgen LU ; Nylander, Tommy LU ; Eliasson, Ann-Charlotte LU ; Shewry, P R ; Tatham, A S and Gilbert, S M
- organization
- publishing date
- 2003
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Repetitive domain, Gliadins, Glutenins, Surface tension
- in
- Journal of Cereal Science
- volume
- 38
- issue
- 2
- pages
- 147 - 156
- publisher
- Elsevier
- external identifiers
-
- wos:000185121800003
- scopus:0041875005
- ISSN
- 0733-5210
- DOI
- 10.1016/S0733-5210(03)00021-3
- language
- English
- LU publication?
- yes
- id
- 8feaa5fa-f68f-4db0-a654-b1f220f04c0e (old id 128307)
- date added to LUP
- 2016-04-01 12:30:28
- date last changed
- 2023-09-02 10:09:07
@article{8feaa5fa-f68f-4db0-a654-b1f220f04c0e,
abstract = {{The surface pressure–molecular area (–A) relationship for spread layers of the high molecular-weight glutenin subunit 1Dx5, a 58 kDa peptide derived from the central repetitive domain of the subunit, and an -gliadin fraction was measured by means of a surface film balance (Langmuir trough). The aqueous phase was a 10 mM acetate buffer, pH 4.0, either with or without 100 mM NaCl. Subunit 1Dx5 generated much higher surface pressures than the 58 kDa peptide, whereas the -gliadin fraction generally gave higher surface pressures than subunit 1Dx5. Furthermore, subunit 1Dx5, but not the 58 kDa peptide or the -gliadin fraction, formed a highly cohesive film. The differences in the interfacial behaviour of subunit 1Dx5 and the 58 kDa peptide were ascribed to significant hydrophobic interactions for the subunit. The reversibility of a compression–expansion cycle was generally greater for the second cycle than for the first. For subunit 1Dx5 and the -gliadins, but not the 58 kDa peptide, the reversibility was increased when NaCl was present in the aqueous phase.}},
author = {{Örnebro, Jörgen and Nylander, Tommy and Eliasson, Ann-Charlotte and Shewry, P R and Tatham, A S and Gilbert, S M}},
issn = {{0733-5210}},
keywords = {{Repetitive domain; Gliadins; Glutenins; Surface tension}},
language = {{eng}},
number = {{2}},
pages = {{147--156}},
publisher = {{Elsevier}},
series = {{Journal of Cereal Science}},
title = {{The behaviour of the high molecular-weight glutenin subunit 1Dx5, the 58 kDa central repetitive domain and a-gliadins at the air-aqueous interface.}},
url = {{http://dx.doi.org/10.1016/S0733-5210(03)00021-3}},
doi = {{10.1016/S0733-5210(03)00021-3}},
volume = {{38}},
year = {{2003}},
}