Abstract
In this study, enzymatic hydrolysis was used to fabricate wheat gliadin hydrolysates (WGHs) for the encapsulation and protection of naringin. The exposure of hydrophilic amino acids decreased the critical micelle concentration (from 0.53 ± 0.02 mg/mL to 0.35 ± 0.03 mg/mL) and improved solubility, which provided amphiphilic conditions for the delivery of naringin. The hydrolysates with a degree of hydrolysis (DH) of 9 % had the strongest binding affinity with naringin, and exhibited the smallest particle size (113.7 ± 1.1 nm) and the highest encapsulation rate (83.2 ± 1.3 %). The storage, heat and photochemical stability of naringin were improved via the encapsulation of micelles. Furthermore, the micelles made up of hydrolysates with a DH of 12 % significantly enhanced the bioavailability of naringin (from 19.4 ± 4.3 % to 46.8 ± 1.4 %). Our experiment provides theoretical support for the utilization of delivery systems based on water-insoluble proteins.