Preparation, characterization, and binding mechanism of quercetin-loaded composite nanoparticles based on zein-soybean protein isolate

• Published in: Food chemistry Vol. 463; no. Pt 3; p. 141359
• Main Authors: Sun, Zhouliang, Li, Dan, Lin, Peiying, Zhao, Yanjie, Zhang, Ji, Sergeeva, Irina, Li, Yang, Zheng, Huanyu
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 18.09.2024
• Subjects: Composite nanoparticles; Controlled release; Encapsulation of quercetin; Soybean protein isolate; Zein; Soybean protein isolate; Encapsulation of quercetin; Zein; Controlled release; Composite nanoparticles
• ISSN: 0308-8146; 1873-7072; 1873-7072
• DOI: 10.1016/j.foodchem.2024.141359

In this study, quercetin (Que) was encapsulated for controlled release during gastrointestinal digestion using zein–soy isolate protein (SPI) composite nanoparticles that were made following an antisolvent precipitation technique. The average particle size of the composite nanoparticles ranged from 182.1 to 230.9 nm, and the polydispersity index (PDI) was small (0.105–0.323). The microstructure revealed that the composite nanoparticles were spherically distributed and that Que. was embedded on the surface of the nanoparticles. Que. has an encapsulation efficiency of up to 93.3 %. Spectrum analysis, molecular docking and zeta potential measurements revealed that the interactions between the composite nanoparticles and Que. occurred mainly through hydrophobic interactions, hydrogen bonding, and electrostatic interactions. Compared with single zein nanoparticles, the composite nanoparticles showed a significant and controlled release of Que. during the whole simulated gastrointestinal digestion process. This study provides a novel method for the development of a controlled-release drug delivery system for controlling the release of Que. [Display omitted] •Adding SPI can improve the dispersion of zein-SPI composite nanoparticles.•The zein-SPI nanoparticles significantly slowed down the release of quercetin.•Que. was combined by hydrogen bonding and hydrophobic interaction with zein-SPI.