TY  - JOUR
AU  - Dahesh, Mohsen
AU  - Banc, Amélie
AU  - Duri, Agnès
AU  - Morel, Marie-Hélène
AU  - Ramos, Laurence
TI  - Polymeric Assembly of Gluten Proteins in an Aqueous Ethanol Solvent
JO  - The journal of physical chemistry  / B
VL  - 118
IS  - 38
SN  - 1520-5207
CY  - Washington, DC
PB  - Soc.
M1  - FZJ-2014-05400
SP  - 11065 - 11076
PY  - 2014
AB  - The supramolecular organization of wheat gluten proteins is largely unknown due to the intrinsic complexity of this family of proteins and their insolubility in water. We fractionate gluten in a water/ethanol mixture (50/50 v/v) and obtain a protein extract which is depleted in gliadin, the monomeric part of wheat gluten proteins, and enriched in glutenin, the polymeric part of wheat gluten proteins. We investigate the structure of the proteins in the solvent used for extraction over a wide range of concentration, by combining X-ray scattering and multiangle static and dynamic light scattering. Our data show that, in the ethanol/water mixture, the proteins display features characteristic of flexible polymer chains in a good solvent. In the dilute regime, the proteins form very loose structures of characteristic size 150 nm, with an internal dynamics which is quantitatively similar to that of branched polymer coils. In more concentrated regimes, data highlight a hierarchical structure with one characteristic length scale of the order of a few nm, which displays the scaling with concentration expected for a semidilute polymer in good solvent, and a fractal arrangement at a much larger length scale. This structure is strikingly similar to that of polymeric gels, thus providing some factual knowledge to rationalize the viscoelastic properties of wheat gluten proteins and their assemblies.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000342396000005
C6  - pmid:25171192
DO  - DOI:10.1021/jp5047134
UR  - https://juser.fz-juelich.de/record/171843
ER  -