Structural studies of adsorbed protein (betalactoglobulin) on natural clay (montmorillonite)
| Autor: | Jérôme Hirschinger, Camille Loupiac, Chloé Roullier-Gall, Régis D. Gougeon, Jésus Raya, Lucie Huault, Philippe Cayot, Cyrielle Maissiat, Ali Assifaoui, Maguy Jaber, Jean-François Lambert, Philippe Jeandet |
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| Přispěvatelé: | Procédés Alimentaires et Physico-Chimie (PAPC), Procédés Alimentaires et Microbiologiques (PAM), Université de Bourgogne (UB)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Université de Bourgogne (UB)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement, LABORATOIRE DE STRESS, DÉFENSES ET REPRODUCTION DES PLANTES (SDRP), Université de Reims Champagne-Ardenne (URCA), Institut de Chimie de Strasbourg, Université de Strasbourg (UNISTRA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Laboratoire d'Archéologie Moléculaire et Structurale (LAMS), Institut de Chimie du CNRS (INC)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Réactivité de Surface (LRS), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut de Chimie du CNRS (INC)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS) |
| Rok vydání: | 2014 |
| Předmět: |
chemistry.chemical_classification
Globular protein General Chemical Engineering Mineralogy General Chemistry Exfoliation joint Fluorescence chemistry.chemical_compound Adsorption Montmorillonite chemistry Chemical engineering Solid-state nuclear magnetic resonance [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Clay minerals Hybrid material |
| Zdroj: | RSC Advances RSC Advances, Royal Society of Chemistry, 2014, 4 (105), pp.61096-61103. ⟨10.1039/C4RA11607K⟩ RSC Advances, 2014, 4 (105), pp.61096-61103. ⟨10.1039/C4RA11607K⟩ |
| ISSN: | 2046-2069 |
| DOI: | 10.1039/c4ra11607k |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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