Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
11027454 | Food Chemistry | 2019 | 37 Pages |
Abstract
One challenge for daidzein delivery is how to efficiently suppress its precipitation/crystallization in a lipid-based system. In this work, whey protein isolate (WPI) with different thermal treatment was employed as a hydrophobic drug crystallization depressor and its interaction mechanism with daidzein was studied. The results indicated WPI aggregated to form nanoparticles (below 300â¯nm) in the presence of daidzein. Thermal denaturing (85â¯Â°C, 20â¯min) improved the binding affinity for daidzein with Kaâ¯=â¯1.165â¯Ãâ¯104â¯Mâ1, about 1.5-fold higher than that of the native protein (Kaâ¯=â¯7.285â¯Ãâ¯103â¯Mâ1). Hydrophobic interaction was the major driving forces based on thermodynamic calculation. The as-obtained protein-based nanocomplexes efficiently inhibited daidzein crystallization, enhancing its solubility at least 2-fold with promoted stability (stable at 4â¯Â°C for at least 2â¯months). These findings provide new ideas for the application of WPI, showing great potential to be directly used in lipid nanocarrier system as crystallization depressor.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Liang Lv, Caili Fu, Fang Zhang, Shaoyun Wang,