Dense Phases of γ-Gliadins in Confined Geometries
| Autor: | Laurence Navailles, Amélie Banc, Jacques Leng, Denis Renard |
|---|---|
| Přispěvatelé: | Laboratoire Charles Coulomb (L2C), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Centre de Recherche Paul Pascal (CRPP), Université de Bordeaux (UB)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Laboratoire du Futur (LOF), Université Sciences et Technologies - Bordeaux 1-RHODIA-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE) |
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
0106 biological sciences
liquid–liquid phase separation Materials science Microfluidics 01 natural sciences 03 medical and health sciences gliadin icroevaporation protein bodies Colloid and Surface Chemistry Phase (matter) Solubility Spectroscopy QD1-999 030304 developmental biology Phase diagram 0303 health sciences Aqueous solution technology industry and agriculture [SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biophysics Solvent Chemistry Chemical engineering Chemistry (miscellaneous) [PHYS.PHYS.PHYS-CHEM-PH]Physics [physics]/Physics [physics]/Chemical Physics [physics.chem-ph] 010606 plant biology & botany Protein adsorption |
| Zdroj: | Colloids and Interfaces, Vol 5, Iss 51, p 51 (2021) Colloids and Interfaces Colloids and Interfaces, MDPI, 2021, 5 (4), pp.51. ⟨10.3390/colloids5040051⟩ Colloids and Interfaces; Volume 5; Issue 4; Pages: 51 |
| ISSN: | 2504-5377 |
| DOI: | 10.3390/colloids5040051⟩ |
| Popis: | International audience; The binary phase diagram of γ-gliadin, a wheat storage protein, in water was explored thanks to the microevaporator, an original PDMS microfluidic device. This protein, usually qualified as insoluble in aqueous environments, displayed a partial solubility in water. Two liquid phases, a very dilute and a dense phase, were identified after a few hours of accumulation time in the microevaporator. This liquid–liquid phase separation (LLPS) was further characterized through in situ micro-Raman spectroscopy of the dilute and dense protein phases. Micro-Raman spectroscopy showed a specific orientation of phenylalanine residues perpendicular to the PDMS surfaces only for the diluted phase. This orientation was ascribed to the protein adsorption at interfaces, which would act as nuclei for the growth of dense phase in bulk. This study, thanks to the use of both aqueous solvent and a microevaporator, would provide some evidence for a possible physicochemical origin of the gliadin assembly in the endoplasmic reticulum of albumen cells, leading to the formation of dense phases called protein bodies. The microfluidic tool could be used also in food science to probe protein–protein interactions in order to build up phase diagrams |
| Databáze: | OpenAIRE |
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