pH-shifting encapsulation of curcumin in egg white protein isolate for improved dispersity, antioxidant capacity and thermal stability.

Curcumin (Cur) has many functions, such as antioxidant and anti-inflammatory. However, its poor solubility and thermal stability at aqueous solutions limit its application in the food industry. In this study, egg white protein isolate (EPI) was complexed with Cur via a pH-shifting method. The effects of ultimate pH (from 5.0 to 7.0) on the physicochemical properties of the complex were studied. Cur could reach 84.4% encapsulation efficiency at pH 6.0. Meanwhile, the EPI complex could remain stable at pH 7.0 after 30 days and protect Cur from thermal degradation, thereby improving the Cur retention rate with the increasing ultimate pH. Compared with those of EPI and free Cur, the antioxidant capacity of the complex was enhanced effectively. The EPI-Cur complex was certified using UV-vis and fluorescence spectra. The fluorescence results indicated that Cur and EPI are combined through a static quenching and with a strong affinity of 1.8 × 10 M at pH 6.0. In summary, this work provides a biocompatible and straightforward method for the development of nanoparticles based on egg white protein isolates, which can be used as a promising carrier for insoluble nutritional compounds.