Interaction of oil bodies proteins with phospholipid bilayers: A molecular level elucidation as revealed by infrared spectroscopy
dc.rights.license | open | en_US |
hal.structure.identifier | Chimie et Biologie des Membranes et des Nanoobjets [CBMN] | |
dc.contributor.author | BOURGEOIS, Christine | |
dc.contributor.author | GOMAA, Ahmed I. | |
dc.contributor.author | LEFEVRE, Thierry | |
hal.structure.identifier | Chimie et Biologie des Membranes et des Nanoobjets [CBMN] | |
dc.contributor.author | CANSELL, Maud | |
dc.contributor.author | SUBIRADE, Muriel | |
dc.date.accessioned | 2020-04-17T09:09:59Z | |
dc.date.available | 2020-04-17T09:09:59Z | |
dc.date.issued | 2018 | |
dc.identifier.issn | 0141-8130 | en_US |
dc.identifier.uri | https://oskar-bordeaux.fr/handle/20.500.12278/4291 | |
dc.description.abstractEn | It is crucial to develop new natural sources of emulsifiers to substitute the synthetic molecules. An ideal emulsifying system exists in plants that is consisting of oil bodies proteins and phospholipids. In this study, Fourier transformed infrared (FTIR) spectroscopy was used to investigate the interactions between oil bodies proteins (OBP) and model phospholipid (PL) membranes. The secondary structure and PL thermotropism were investigated. Different PL varying in chain length and polar head were used including two zwitterionic phospholipids, dimyristoylphosphatidylcholine and dioleoylphosphatidylcholine, and two anionic phospholipids, dimyristoylphosphatidylglycerol, dipalmitoylphosphatidylglycerol. The changes in lipid physical state and protein denaturation were investigated as a function of temperature from 20 to 80 °C. OBP in solution is composed of unordered structures and beta-sheets with signs of aggregation. Anionic PL interacts with OBP whereas zwitterionic PL does not or only slightly interacts with the protein. Unsaturated PL promoted the alpha-helix structure in OBP. The interactions between OBP and PL depended on the protein charge inducing different protein conformations. Overall, the study showed that OBP and commercial anionic phospholipids have a potential in developing stable emulsifier for food industry. | |
dc.language.iso | EN | en_US |
dc.subject.en | Oil body proteins | |
dc.subject.en | Phospholipids | |
dc.subject.en | Emulsions | |
dc.subject.en | FTIR | |
dc.title.en | Interaction of oil bodies proteins with phospholipid bilayers: A molecular level elucidation as revealed by infrared spectroscopy | |
dc.type | Article de revue | en_US |
dc.identifier.doi | 10.1016/j.ijbiomac.2018.10.211 | en_US |
dc.subject.hal | Chimie/Matériaux | en_US |
bordeaux.journal | International journal of biological macromolecules | en_US |
bordeaux.page | 873-881 | en_US |
bordeaux.volume | 122 | en_US |
bordeaux.hal.laboratories | Institut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248 | |
bordeaux.institution | Bordeaux INP | en_US |
bordeaux.institution | Université de Bordeaux | en_US |
bordeaux.peerReviewed | oui | en_US |
bordeaux.inpress | non | en_US |
hal.identifier | hal-02545553 | |
hal.version | 1 | |
hal.date.transferred | 2020-04-17T09:10:04Z | |
hal.export | true | |
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