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The behaviour of the high molecular-weight glutenin subunit 1Dx5, the 58 kDa central repetitive domain and a-gliadins at the air-aqueous interface.

Örnebro, Jörgen LU ; Nylander, Tommy LU ; Eliasson, Ann-Charlotte LU ; Shewry, P R; Tatham, A S and Gilbert, S M (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:
author
organization
publishing date
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
2007-07-19 11:49:09
date last changed
2018-05-29 10:32:13
@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},
  keyword      = {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},
  volume       = {38},
  year         = {2003},
}