Gel properties of heat-induced transparent hydrogels from ovalbumin by acylation modifications

In this paper, the effects of acylation modification on the gel behavior of ovalbumin (OVA) under heating induction have been investigated. From the obtained results, the acylated OVA hydrogels exhibited superior gelation properties than the native OVA hydrogels (NOVA-G) in terms of light transmission, gel hardness, resilience and water holding capacity. SEM revealed acylation modifications effectively promoted the formation of uniform and dense network structure of OVA hydrogels. The main intermolecular forces of the acylation-modified OVA hydrogels were hydrophobic interactions and hydrogen bonding. FTIR showed that acylation modifications caused 26.2% decrease in α-helix and 59.2% increase in β-sheet content compared to NOVA-G. Furthermore, in-vitro release experiments showed that the release rate of curcumin from acylated OVA hydrogels was significantly delayed. Moreover, the above results have shown that acylation modifications can be considered as an effective method to improve the gelation as well as drug release properties of protein hydrogels.