6533b854fe1ef96bd12ae163
RESEARCH PRODUCT
Structural studies of adsorbed protein (betalactoglobulin) on natural clay (montmorillonite)
Jérôme HirschingerCamille LoupiacChloé Roullier-gallRégis D. GougeonJésus RayaLucie HuaultPhilippe CayotCyrielle MaissiatAli AssifaouiMaguy JaberJean-françois LambertPhilippe Jeandetsubject
chemistry.chemical_classificationGlobular proteinGeneral Chemical EngineeringMineralogyGeneral ChemistryExfoliation jointFluorescencechemistry.chemical_compoundAdsorptionMontmorillonitechemistryChemical engineeringSolid-state nuclear magnetic resonance[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyClay mineralsHybrid materialdescription
International audience; In this work, the adsorption of a small globular protein (betalactoglobulin, BLG), on a natural montmorillonite clay (Mt) was investigated in acidic buffer (pH = 3). The combination of different characterization techniques such as zetametry, X-ray diffraction, transmission electronic microscopy, fluorescence and solid state nuclear magnetic resonance spectroscopies shed light on the interaction mechanism between the clay mineral and the proteins. For low BLG concentration, a slight increase of the interlayer spacing of the clay mineral was noticed as well as structural changes of the protein. In contrast, as the concentration of BLG increased, the adsorption led to a partial exfoliation of the clay mineral, accompanied with significant secondary structural changes of the protein characterized by a loss of β-sheet organization. Altogether, our results revealed an unexpected adsorption scheme where the increase of the BLG/Mt weight ratio of the hybrid material leads to a partial exfoliation of the Mt, but at the expense of the protein native structure.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2014-01-01 | RSC Adv. |