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(16) Production(s) de DAHESH M.
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Novel gels from wheat gluten proteins 
Auteur(s): Dahesh M., Banc A., Duri Agnes, Morel Marie Helene, Ramos L.
Conference: School of chemistry and chemical engineering, Shandong university (Shandong, CN, 2014)
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Novel gels from wheat gluten proteins
Auteur(s): Dahesh M., Banc A., Duri Agnes, Morel Marie Helene, Ramos L.
Conference: Laboratoire de physique, ENS Lyon (Lyon, FR, 2014)
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Structuration and rheological properties of gels made from gluten proteins
Auteur(s): Dahesh M., Banc A., Duri Agnes, Morel Marie Helene, Ramos L.
Conference: Laboratoire du futur (Bordeaux, FR, 2014)
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Novels gels from wheat gluten proteins
Auteur(s): Dahesh M., Banc A., Duri-Bechemilh Agnès, Morel Marie Helene, Ramos L.
Conference: 3. Journée scientifique du labex NUMEV (solutions numériques, matérielles et modélisation pour l’environnement et le vivant) (Montpellier, FR, 2014-07-01)
Ref HAL: hal-01606486_v1
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Résumé: Novels gels from wheat gluten proteins. 3. Journée scientifique du labex NUMEV (solutions numériques, matérielles et modélisation pour l’environnement et le vivant)
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Microcellular foams made from gliadin
Auteur(s): Quester S., Dahesh M., Strey R.
(Article) Publié:
Progress In Colloid And Polymer Science, vol. 292 p.2385-2389 (2014)
Texte intégral en Openaccess : 
Ref HAL: hal-01227417_v1
DOI: 10.1007/s00396-014-3317-6
WoS: 000341489900034
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6 Citations
Résumé: We have generated closed-cell microcellular foams from gliadin, an abundantly available wheat storage protein. The extraction procedure of gliadin from wheat gluten, which involves only the natural solvents water and ethanol, respectively, is described with emphasis on the precipitation step of gliadin which results in a fine dispersion of mostly spherical, submicron gliadin particles composed of myriad of protein molecules. A dense packing of these particles was hydrated and subjected to an atmosphere of carbon dioxide or nitrogen in a high-pressure cell at 250 bar. Subsequent heating to temperatures close to but still below 100 A degrees C followed by sudden expansion and simultaneous cooling resulted in closed-cell microcellular foam. The spherical gliadin templates along with the resulting foam have been analyzed by scanning electron microscope (SEM) pictures. The size distribution of the primary particles shows diameters peaked around 0.54 mu m, and the final foam cell size peaks around 1.2 mu m, at a porosity of about 80 %. These are the smallest foam cell sizes ever reported for gliadin. Interestingly, the cell walls of these microcellular foams are remarkably thin with thicknesses in the lower nanometer range, thus nourishing the hope to be able to reach gliadin nanofoam.
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Polymeric Assembly of Gluten Proteins in an Aqueous Ethanol Solvent
Auteur(s): Dahesh M., Banc A., Duri Agnès, Morel Marie-Hélène, Ramos L.
(Article) Publié:
Journal Of Physical Chemistry B, vol. 118 p.11065 (2014)
Texte intégral en Openaccess : 
Ref HAL: hal-01071076_v1
Ref Arxiv: 1409.0744
DOI: 10.1021/jp5047134
WoS: 000342396000005
Ref. & Cit.: NASA ADS
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34 Citations
Résumé: 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 (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 multi-angle 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 protein 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 semi-dilute polymer in good solvent, and a fractal arrangement at 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.
Commentaires: J. Phys. Chem. B 2014, 118, 11065
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Structuration and Rheological Properties of Gels made from Gluten Proteins
Auteur(s): Dahesh M., Banc A., Duri-Bechemilh Agnès, Morel Marie Helene, Ramos L.
Conference: 9. Annual European Rheological Conference (AERC 2014) (Karlsruhe, DE, 2014-04-08)
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Résumé: Structuration and Rheological Properties of Gels made from Gluten Proteins. 9. Annual European Rheological Conference (AERC 2014)
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