In-situ grafting of dextran on oil body associated proteins at the oil–water interface through maillard glycosylation: Effect of dextran molecular weight

Oil bodies, which are lipid-storage organelles in plant seeds, are stabilized by monolayer of phospholipids and oil body associated proteins (OBAPs). OBAPs have unique interfacial characteristics but poor water-solubility because they contain long hydrophobic segments. In this paper, dextran with different molecular weights (5, 10, and 20 kDa) was grafted onto the C- and N-terminal ends of OBAPs through in situ Maillard reaction on the surface of oil bodies. Grafting of dextran increases the length of the hydrophilic region of OBAPs, which improves their solubility and function as interfacial stabilizers. Changes in chemical bonds after grafting were observed via confocal-Raman microscopy. After de-lipidization, the physicochemical properties of OBAPs–dextran conjugates were analyzed using solubility and infrared spectroscopy. The interfacial behavior was evaluated using critical micelle concentration and interfacial rheology. The results showed that grafting of dextran improved the solubility of the OBAPs by 20-fold. The contents of α-helix and β-sheet in the OBAPs–dextran conjugates decreased, when compared with OBAPs. The critical micelle concentration of OBAPs–dextran conjugates ranged from 1.20 to 4.92 μg/mL. Grafting of dextran, especially high molecular weight, improved the capacity of the OBAPs to increase the interfacial pressure. Our results provide an efficient and eco-friend method for modification of membrane proteins. [Display omitted] •Glycosylation at the oil–water interface through Maillard reaction is green and efficient.•Water-solubility of oil body associated proteins increased 20-fold after glycosylation.•Obtained protein–dextran conjugates have a very low critical micelle concentration.•Glycosylation at the interface is monitored using confocal-Raman spectroscopy in situ.