Designation and characterization of cold-set egg white protein/dextran sulfate hydrogel for curcumin entrapment. (1st September 2023)

• Record Type: Journal Article
• Authors: Liu, Jingbo; Chai, Jiale; Yuan, Yixin; Wu, Xinling; Gong, Lingling; Yu, Peixin; Liu, Pengyu; Zhang, Ting; Shang, Xiaomin
• Is Part Of: Food chemistry. Volume 419(2023)
• Publication Date: 2023-09-01
• Subjects: Egg white protein -- Sulfated polysaccharide -- Acid-induced gelation -- Transglutaminase -- Controlled-release -- Microstructure; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2023.136038
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: Soluble egg white protein/sulfated polysaccharide complexes were obtained at pH 12. Soluble protein/polysaccharide complexes acted as building blocks of cold-set gels. The presence of TGase further enhanced the mechanical properties of cold-set gel. The release of curcumin from cold-set gel exhibits an obvious slow-release effect. 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.