Ultrasound-assisted pH-shifting remodels egg-yolk low-density lipoprotein to enable construction of a stable aqueous solution of vitamin D3

Egg-yolk low-density lipoprotein (LDL) has a natural liposome structure. Using ultrasound-assisted pH-shifting (pH 12), a naturally safe and stable aqueous solution of vitamin D-3 (VD3) was constructed employing LDL as the carrier. Images from electron microscopy showed that pH-shifting remodeled LDL molecules, resulting in a dramatic reduction in particle size (similar to 50%) and an increase in specific surface area, which reduced the turbidity (27.7%) and provided new interfaces for VD3 loading. Fluorescence analyses showed that the binding of VD3 to LDL under pH-shifting was strong, involved quenching, and the binding constant was 6.19 x 10(4) M-1. Thermogravimetric analysis and Fourier transform-infrared spectroscopy showed that pH-shifting hydrolyzed the esters in LDL to fatty acid salts, and the maximum weight loss of LDL occurred from 381.9 degrees C to 457.0 degrees C. Ultrasonic treatment enhanced the binding of LDL and VD3 (binding constant increased to 2.56 x 10(7) M-1), reduced the particle size, and increased the potential of the complex between LDL and VD3, thereby resulting in the improvement of solution stability and storage stability of VD3. Ultrasound-assisted pH-shifting could remodel LDL to construct a stable aqueous solution of VD3, which showed the potential of LDL as a carrier for lipid-soluble components.