Complexing with fibrillated glutenin and orange peel pectin improves the aqueous dispersion and storage stability of hesperitin/hesperidin

Hesperitin (Ht) and hesperidin (Hd) have a variety of biological activities, but their applications are limited due to the poor aqueous dispersion, weak stability and low bioavailability. In this study, a complex coacervate, formed by glutenin heated at pH 2, 80 °C for 8 h and orange peel pectin (P), was used as a carrier to enhance the water dispersibility of Ht/Hd, and their release behavior in vitro were investigated. The main driving forces for the complexes of Ht/Hd with glutenin (Glu) or fibrillated glutenin (Glu-F) were hydrogen bonding and hydrophobic forces. However, the enthalpy change of the interaction of the fibrillated glutenin with Ht/Hd was reduced, implying the formation of a more stable Ht/Hd-Glu-F complex. Furthermore, the optimum mass parameter ratio of Ht/Hd:P:Glu-F obtained from orthogonal experiments was 5:4:40 at pH 6. Both Ht and Hd were almost insoluble in water (pH 6), while the formation of the Ht-Glu-F-P and Hd-Glu-F-P complexes increased the solubility of the almost insoluble Ht and Hd to 102.16 ± 4.82 and 220.57 ± 10.82 μg/mL, respectively. After 30 days of storage, the particle size of the emulsions formed by Ht-Glu-F-P and Hd-Glu-F-P complexes increased from 171.90 to 174.84 nm to 231.82 and 219.81 nm, respectively, which had better storage stability than those formed from Ht/Hd-Glu-P complexes. The increased intermolecular repulsion caused by fibrillation modification improved the stability of the delivery system. These results provide a unique method for improving the aqueous dispersion and storage stability of Ht/Hd.