As a lipophilic flavonol, quercetin has low bioavailability, which limits its application in foods. This work aimed to prepare a hordein-based system to deliver quercetin. We constructed hordein-whey isolate protein fibril (WPIF) complexes (H-Ws) by anti-solvent precipitation method at pH 2.5. The TEM results of the complexes showed that spherical-like hordein particles were wrapped in WPIF clusters to form an interconnected network structure. FTIR spectra revealed that hydrogen bonds and hydrophobic interactions were the main driving forces for the complex formation. H-W1 (the mass ratio of hordein to WPIF was 1:1) with a three-phase contact angle of 70.2° was chosen to stabilize Pickering emulsions with oil volume fractions (φ) of 40-70%. CLSM images confirmed that the oil droplets were gradually embedded in the three-dimensional network structure of H-W1 with the increase in oil volume fraction. The emulsion with φ = 70% showed a tight gel structure. Furthermore, this emulsion exhibited high encapsulation efficiency (97.8%) and a loading capacity of 0.2%, demonstrating the potential to deliver hydrophobic bioactive substances. Compared with free quercetin, the bioaccessibility of the encapsulated quercetin (35%) was significantly improved. This study effectively promoted the application of hordein-based delivery systems in the food industry.
Keywords: Pickering emulsion; hordein; quercetin; whey protein isolate fibril.