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Updated: Feb 8, 2026

Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro
Published on: April 8, 2020
Insight on the interaction between chickpea protein isolate and dextran: Structural analysis, functional
Jing Zhang1, Yan Shi2, Yueming Hu1
1State Key Laboratory of Food Science and Resources, Nanchang University, 235 Nanjing East Road, Nanchang, Jiangxi 330047, China.
None:
Water-in-oil-in-water (W/O/W) emulsions were commonly used for the co-encapsulation of hydrophilic and hydrophobic compounds. However, the stability remained a significant challenge. This study employed a non-covalent chickpea protein isolate-dextran (CPI-Dex) complex to construct a stable W/O/W emulsion. The interaction of the CPI-Dex complex and its effect on the physical stability and encapsulation efficiency of the W/O/W emulsion were investigated. Multispectral analyses showed that Dex induced structural changes in CPI, promoting its structural unfolding and exposure of hydrophobic groups. Molecular docking showed that CPI interacts with Dex mainly through hydrogen bonding and the CPI-Dex complex were highly stable. The emulsification and interfacial properties of the CPI-Dex complex were improved. At a CPI-Dex ratio of 1:3, the emulsion exhibited a superior physical stability and viscosity. Moreover, this emulsion demonstrated the highest encapsulation efficiency of chlorogenic acid (81.08 ± 0.87 %) and lutein (92.21 ± 0.08 %). In summary, this study was beneficial in corroborating the ability of Dex in improving the emulsification and interfacial properties of CPI and improving the performance of the co-encapsulated W/O/W emulsion.
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