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(16) Production(s) de DAHESH M.
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Structuration and mechanical properties of gels made from gluten proteins 
Auteur(s): Dahesh M., Banc A., Duri-Bechemilh Agnès, Morel Marie Helene, Ramos L.
(Affiches/Poster)
International soft matter conference (ISMC) (Rome, IT), 2013Texte intégral en Openaccess : 
Ref HAL: hal-01601702_v1
Exporter : BibTex | endNote
Résumé: Wheat gluten proteins are among the most complex protein networks in nature, due in particular to their poor solubility in water and to their viscoelastic behavior. Gluten networks are often considered as transient networks comprising extensible biopolymer segments of flexible or semiflexible chains between junction points. However, the exact structure of the network, the nature of the junction points and the way it get structured under shear remain to be clarified. Here we report the visco-elastic behavior of model systems composed of gluten proteins near gelation. We build model systems by dispersing in ethanol-water mixtures two major protein groups, gliadins and glutenins, that we have purified from gluten. Rheological properties show a slow evolution over time scales of the order of days of the linear frequency dependence complex modulus of the samples, with a concentration-dependent liquid to solid transition. Interestingly, we find that all data acquired at different protein concentrations and different times after sample preparation can be scaled onto a master curve showing a cross-over from a soft solid behavior at low frequency to a visco-elastic fluid at high frequency.Rheological data are completed by scattering experiments in order to elucidate the complex structure of the materials. For gel samples, the scattering profiles display at small length scales features typical of polymer and evidences at larger length scale a fractal structure that we interpret as being due to the highly disordered state of the junction points. Biochemical assays are also performed to elucidate the origin of the sample aging.
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Rheology of model systems made from gluten proteins near the liquid-solid transition
Auteur(s): Dahesh M. , Banc A., Duri Agnés, Morel Marie-Hélène, Ramos L.
Conference: Annual ESMI/Softcomp meeting 2013 (Rimini, IT, 2013-05-27)
Ref HAL: hal-00831515_v1
Exporter : BibTex | endNote
Résumé: Wheat gluten proteins are insoluble in water and are among the most complex protein networks in nature. In spite of their extensively use in particular for bread making, their viscoelastic properties and their structuration are still largely unknown. Here we report the visco-elastic behavior of model systems composed of gluten proteins near the liquid-solid transition. We build model systems by dispersing in ethanol-water mixtures two major protein groups, gliadin and glutenin, that we have purified from gluten. We find a slow evolution over time scales of the order of days of the linear frequency dependence complex modulus of the samples. Interestingly, we find that all data acquired at different protein concentrations and different times after sample preparation can be scaled onto a master curve, showing a cross-over from a soft solid at low frequency to a visco-elastic fluid at high frequency. We are currently using scattering techniques to unveil the peculiar structure of the protein network that would lead to the self-similar visco-elasticity.
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