Langmuir, Vol.29, No.26, 8222-8232, 2013
Influence of Vitamin E Acetate and Other Lipids on the Phase Behavior of Mesophases Based on Unsaturated Monoglycerides
The phase behavior of the ternary unsaturated monoglycerides (UMG)-DL-alpha-tocopheryl acetate-water system has been studied. The effects of lipid composition in both bulk and dispersed lyotropic liquid crystalline phases and microemulsions were investigated. In excess water, progressive addition of DL-alpha-tocopheryl acetate to a binary UMG mixture results in the following phase sequence: reversed bicontinuous cubic phase, reversed hexagonal (H-II) phase, and a reversed microemulsion. The action of DL-alpha-tocopheryl acetate is then compared to that of other lipids such as triolein, limonene, tetradecane, and DL-alpha-tocopherol. The impact of solubilizing these hydrophobic molecules on the UMG-water phase behavior shows some common features. However, the solubilization of certain molecules, like DL-a-tocopherol, leads to the presence of the reversed micellar cubic phase (space group number 227 and symmetry Fd (3) over barm) while the solubilization of others does not. These differences in phase behavior are discussed in terms of physical-chemical characteristics of the added lipid molecule and its interaction with UMG and water. From an applications point of view, phase behavior as a function of the solubilized content of guest molecules (lipid additive in our case) is crucial since macroscopic properties such as molecular release depend strongly on the phase present The effect of two hydrophilic emulsifiers, used to stabilize the aqueous dispersions of UMG, was studied and compared Those were Pluronic F127, which is the most commonly used stabilizer for these kinds of inverted type structures, and the partially hydrolyzed emulsifier lecithin (Emultop EP), which is a well accepted food grade emulsifier. The phase behavior of particles stabilized by the partially hydrolyzed lecithin is similar to that of bulk sample at full hydration, but this emulsifier interacts significantly with the internal structure and affects it much more than F127.