Ovalbumin amyloid-like fibrils/resveratrol self-assembling hydrogel: Preparation, characterization and formation mechanism

Abstract

Food protein amyloid-like fibrils can significantly increase solution viscosity and promote the formation of entangled gel network due to its high stiffness and extreme aspect ratios. In this study, the ability of hydrophobic resveratrol (RES) deposited on the surface of the ovalbumin (OVA) amyloid-like fibrils (OVAF) to form a new self-assembling hydrogel was explored. The results showed that the simple mixing of RES and OVAF at pH 6.5 can successfully drive the formation of hybrid hydrogels through molecular self-assembly. The interactions between OVAF and RES were confirmed by the results of transmission electron microscope and fluorescence spectra. Non-covalent interactions including hydrophobic interactions and hydrogen bonds played an important role in the formation of the OVAF/RES self-assembling hydrogels. Furthermore, the OVAF/RES hydrogel showed a dense structure, high water holding capacity and remarkable rheological properties. The viscosity and storage modulus of the hybrid hydrogels increased with the increase of the RES and OVAF concentrations. After gastrointestinal digestion, some fibrous structures in the OVAF/RES hydrogels remained, which allowed for continuous release of RES. In summary, the OVAF/RES hybrid hydrogels with tunable structures, encapsulation ability and self-assembly characteristics are expected to be candidates for the delivery of hydrophobic active polyphenols in the food industry.