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dc.rights.licenseopenen_US
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorBOURGEOIS, Christine
dc.contributor.authorGOMAA, Ahmed I.
dc.contributor.authorLEFEVRE, Thierry
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorCANSELL, Maud
dc.contributor.authorSUBIRADE, Muriel
dc.date.accessioned2020-04-17T09:09:59Z
dc.date.available2020-04-17T09:09:59Z
dc.date.issued2018
dc.identifier.issn0141-8130en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/4291
dc.description.abstractEnIt 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.isoENen_US
dc.subject.enOil body proteins
dc.subject.enPhospholipids
dc.subject.enEmulsions
dc.subject.enFTIR
dc.title.enInteraction of oil bodies proteins with phospholipid bilayers: A molecular level elucidation as revealed by infrared spectroscopy
dc.typeArticle de revueen_US
dc.identifier.doi10.1016/j.ijbiomac.2018.10.211en_US
dc.subject.halChimie/Matériauxen_US
bordeaux.journalInternational journal of biological macromoleculesen_US
bordeaux.page873-881en_US
bordeaux.volume122en_US
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
hal.identifierhal-02545553
hal.version1
hal.date.transferred2020-04-17T09:10:04Z
hal.exporttrue
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