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(80) Production(s) de BANC A.
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Spontaneous gelation of wheat gluten proteins in a food grade solvent 
Auteur(s): Ramos L. , Dahesh M., Banc A., Duri Agnés, Morel Marie-Hélène
Conference: International Symposium on Food Rheology and Structure (Zurich, CH, 2015-06-09)
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Résumé: Producing wheat gluten gels with tunable mechanical properties via simple sol-gel routes would facilitate their processing into plant protein-rich food products. However, standard gluten is a very elastic mass with a high concentration of proteins in water and is hardly processable except using high shear harsh extrusions. The wheat proteins are responsible for the viscoelastic properties of standard gluten and dough and are among the most complex proteins families, with extremely broad polymorphisms and polydispersities. They are moreover insoluble in water, rendering rational studies difficult. Thanks to a novel protocol for the gluten proteins extraction that we have recently developed, stable ethanolic suspensions of gluten proteins are obtained for a wide range of protein concentrations. In this talk, we will present the viscoelasticity of those suspensions and show that they exhibit a spontaneous and concentration-dependent gelation, which we find to be driven by the slow formation of hydrogen bonds. We successfully rationalize our data using percolation models and relate the viscoelasticity of the gels to their fractal dimension measured by scattering techniques. The novel gluten gels display self-healing properties and their elastic plateaus cover several decades, from 10-2 to 104 Pa. In particular very soft gels as compared to standard hydrated gluten, suitable for processing, can be produced.
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Polymeric assembly of gluten proteins in an aqueous ethanol solvent
Auteur(s): Banc A., Dahesh M., Duri Agnés, Morel Marie-Hélène, Ramos L.
Conference: International Symposium on Food Rheology and Structure (Zurich, CH, 2015-06-08)
Ref HAL: hal-01164758_v1
Exporter : BibTex | endNote
Résumé: he 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.
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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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