%0 Journal Article
%T Insight into gluten structure in a mild chaotropic solvent by asymmetrical flow field-flow fractionation (AsFlFFF) and evidence of non-covalent assemblies between glutenin and ω-gliadin
%+ Ingénierie des Agro-polymères et Technologies Émergentes (UMR IATE)
%+ Laboratoire Charles Coulomb (L2C)
%+ Ecole d'Ingénieurs de Purpan (INP - PURPAN)
%+ Chimie Agro-Industrielle (CAI)
%+ Paris-Saclay Food and Bioproduct Engineering (SayFood)
%A Morel, Marie-Hélène
%A Pincemaille, Justine
%A Chauveau, Edouard
%A Louhichi, Ameur
%A Violleau, Frédéric
%A Menut, Paul
%A Ramos, Laurence
%A Banc, Amélie
%Z Doctoral School GAIA and the Labex Numev (ANR-10-LAB-20) for the funding of the PhD Grant ; scientific council of Montpellier SupAgro
%< avec comité de lecture
%@ 0268-005X
%J Food Hydrocolloids
%I Elsevier
%V 103
%P 105676
%8 2020-06
%D 2020
%R 10.1016/j.foodhyd.2020.105676
%Z Chemical Sciences/Theoretical and/or physical chemistry
%Z Life Sciences [q-bio]/Food and NutritionJournal articles
%X Wheat gluten, one of the most complex viscoelastic protein networks in nature, is unique to get the specific texture of bread. Due to its complex protein composition, its insolubility in most solvents and the very high molar mass of half of the proteins (glutenin, the other half being gliadin), the architecture of the network is still not well understood. In this work, we have investigated model gluten protein extracts with contrasted compositions in glutenin and gliadin solubilized in a mild chaotropic solvent: ethanol/water (50/50 v/v). The samples display a liquid-liquid phase separation with an upper critical solution temperature that depends on the protein composition. The phase diagrams are consistent with the presence of supramolecular assemblies of proteins. To confirm the presence of these assemblies and fully characterize the objects dispersed in ethanol/water, we have used an asymmetrical flow field-flow fractionation (AsFlFFF) setup coupled with differential refractive index, multi-angle light scattering and dynamic light scattering detections to probe very dilute protein suspensions. We have identified three classes of objects, with distinctive molar mass, characteristic size and conformation: protein monomers, polymeric structures, and very loose protein assemblies with molar mass larger than 2.10 6 g/mol. A molecular characterization of the species by size exclusion chromatography in a denaturing solvent shows that polymers and assemblies are mainly composed of glutenin and ω-gliadin. The high content of ω-gliadin, devoid of cysteines, indicates the importance of non-covalent interactions involved in protein assemblies and might play a major role in gluten rheology
%G English
%2 https://hal.science/hal-02481505/document
%2 https://hal.science/hal-02481505/file/VersionHAL-Morel2020FoodHydrocolloids.pdf
%L hal-02481505
%U https://hal.science/hal-02481505
%~ CIRAD
%~ AGROPARISTECH
%~ CNRS
%~ IATE
%~ L2C
%~ UNIV-PARIS-SACLAY
%~ AGREENIUM
%~ MIPS
%~ SABP
%~ BA
%~ AGROPARISTECH-ORG
%~ AGROPARISTECH-SPAB
%~ UNIV-MONTPELLIER
%~ INSTITUT-AGRO-MONTPELLIER
%~ INRAE
%~ SAYFOOD
%~ TEST-HALCNRS
%~ INRAEOCCITANIEMONTPELLIER
%~ UNIVERSITE-PARIS-SACLAY
%~ ANR
%~ GS-ENGINEERING
%~ GS-BIOSPHERA
%~ MICA-UNITES
%~ TOULOUSE-INP
%~ UT3-INP
%~ UT3-TOULOUSEINP
%~ UM-2015-2021
%~ CAI
%~ RESEAU-EAU
%~ INSTITUT-AGRO
%~ PUBLIS-EC-IA-MTP
%~ PUBLIS-EC-IA
%~ ICT-CHIMIE
%~ EIPURPAN