Interaction of oil bodies proteins with phospholipid bilayers: A molecular level elucidation as revealed by infrared spectroscopy
Langue
EN
Article de revue
Ce document a été publié dans
International journal of biological macromolecules. 2018, vol. 122, p. 873-881
Résumé en anglais
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, ...Lire la suite >
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.< Réduire
Mots clés en anglais
Oil body proteins
Phospholipids
Emulsions
FTIR
Unités de recherche