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Scaling Properties of Gelling Systems in Nonlinear Shear Experiments
Auteur(s): Louhichi A., Morel Marie-Hélène, Ramos L., Banc A.
(Article) Publié:
Acs Macro Letters, vol. p.826-831 (2024)
Ref HAL: hal-04629902_v1
DOI: 10.1021/acsmacrolett.4c00121
Exporter : BibTex | endNote
Résumé: We study model near-critical polymer gelling systems made of gluten protein dispersions stabilized at different distances from the gel point. We impose different shear rates and follow the time evolution of the stress. For sufficiently large shear rates, an intermediate stress overshoot is measured before reaching the steady state. We evidence self-similarity of the stress overshoot as a function of the applied shear rate for samples with various distances from the gel point, which is related to the elastic energy stored by the samples, as for dense systems close to the jamming transition. In concordance with the findings for glassy and jammed systems, we also measure that the stress after flow cessation decreases as a power law with time, with a characteristic relaxation time that depends on the shear rate previously imposed. These features revealed in nonlinear rheology could be the signature of a mesoscopic dynamics, which would depend on the extent of gelation.
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Delicate Analysis of Interacting Proteins and Their Assemblies by Flow Field-Flow Fractionation Techniques
Auteur(s): Urbes Aurélien, Morel Marie-Hélène, Ramos L., Violleau Frédéric, Banc A.
(Article) Publié:
Biomacromolecules, vol. p. (2024)
Ref HAL: hal-04613885_v1
DOI: 10.1021/acs.biomac.4c00103
Exporter : BibTex | endNote
Résumé: We study the efficiency of several asymmetrical flow field-flow fractionation (AF4) techniques to investigate self-associating wheat gluten proteins. We compare the use of a denaturing buffer including sodium dodecyl sulfate (SDS) and a mild chaotropic solvent, water/ethanol, as the eluent, on a model gluten sample. Through a thorough analysis of the data obtained from coupled light scattering detectors and with the identification of molecular composition of the eluted protein, we evidence coelution events in several conditions. We show that the focus step used in conventional AF4 with the SDS buffer leads to the formation of aggregates that coelute with monomeric proteins. By contrast, a frit-inlet device enables the fractionation of individual wheat proteins in the SDS buffer. Interestingly conventional AF4, using water/ethanol as eluent, is an effective method for fractionating gluten proteins and their complex dynamic assemblies, which involve weak forces and are composed of both monomeric and polymeric proteins.
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Water-Driven Sol–Gel Transition in Native Cellulose/1-Ethyl-3-methylimidazolium Acetate Solutions
Auteur(s): Mohamed Yunus Roshan Akdar, Koch Marcus, Dieudonne-George P., Truzzolillo D., Colby Ralph, Parisi Daniele
(Article) Publié:
Acs Macro Letters, vol. 13 p.219-226 (2024)
Ref HAL: hal-04426657_v1
DOI: 10.1021/acsmacrolett.3c00710
Exporter : BibTex | endNote
Résumé: The addition of water to native cellulose/1-ethyl-3methylimidazolium acetate solutions catalyzes the formation of gels, where polymer chain-chain intermolecular associations act as cross-links. However, the relationship between water content (Wc), polymer concentration (Cp), and gel strength is still missing. This study provides the fundamentals to design water-induced gels. First, the sol-gel transition occurs exclusively in entangled solutions, while in unentangled ones, intramolecular associations hamper interchain cross-linking, preventing the gel formation. In entangled systems, the addition of water has a dual impact: at low water concentrations, the gel modulus is water-independent and controlled by entanglements. As water increases, more cross-links per chain than entanglements emerge, causing the modulus of the gel to scale as Gp ∼ C p^2 Wc^3.0±0.2. Immersing the solutions in water yields hydrogels with noncrystalline, aggregate-rich structures. Such water-ionic liquid exchange is examined via Raman, FTIR, and WAXS. Our findings provide avenues for designing biogels with desired rheological properties.
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