Comparative study of glycyrrhizin interaction with plant-derived proteins for encapsulation and delivery of naringenin: Role of prolamins

This study evaluated dipotassium glycyrrhizinate (DG) modification on four distinct plant-based alternative proteins: legume-derived faba bean protein (mainly globulins), oilseed pumpkin protein (mainly globulins), pseudocereal buckwheat protein (mainly globulins and few prolamins), and cereal zein (exclusive prolamins), to enhance delivery efficiency of naringenin. Through pH-shifting preparation, DG significantly enhanced protein solubility and naringenin encapsulation efficiency (~78.0–98.1 %), particularly in prolamin-rich zein showing 117.6 % solubility increase and 13.0-fold efficiency improvement (from 5.6 % to 78.0 %). Molecular docking revealed that hydrophobic and electrostatic interactions were the key drivers of DG's effects, with prolamins exhibiting greater structural changes under DG modification. Additionally, all DG-modified proteins enhanced naringenin bioaccessibility. These findings highlight DG's potential as a versatile modifier for plant-derived alternative proteins, particularly those rich in prolamins, with promising applications in functional foods.