Designation and characterization of cold-set egg white protein/dextran sulfate hydrogel for curcumin entrapment

Abstract

This study aimed to design a cold-set hydrogel of egg white protein (EWP) with good mechanical properties for encapsulating curcumin. Dextran sulfate (DS) and transglutaminase (TGase) were used to control the aggregation and gelation behavior of EWP at preheating step and gelation step, respectively. The optimum soluble protein aggregate size was obtained in the EWP/DS mixture at a mass ratio of 10 under 85 °C preheated (HED₁₀). The presence of TGase further enhanced the cross-linking degree between protein aggregates during the gelation step. The highest gel hardness was found in HED₁₀ hydrogel with TGase, which is almost 10 times the pure EWP gel. Besides, the HED hydrogels effectively slowed down the release rate of curcumin in gastrointestinal digestion. This work provides a theoretical basis for the development of cold-set EWP hydrogel with good mechanical strength by sulfated polysaccharide addition and TGase cross-linking as encapsulation delivery systems.

Keywords: Acid-induced gelation; Controlled-release; Egg white protein; Microstructure; Sulfated polysaccharide; Transglutaminase.