Fabrication of curcumin-loaded pea protein isolate-quillaja saponin-tannic acid self-assembled nanoparticles by tuning non-covalent interactions: Enhanced physicochemical, interfacial and emulsifying properties

单宁酸 豌豆蛋白 化学 姜黄素 共价键 纳米颗粒 化学工程 戊二醛 热稳定性 色谱法 皮克林乳液 疏水效应 核化学 纳米技术 材料科学 生物化学 有机化学 食品科学 工程类
作者
Xin Qiao,Yanguang Jiang,Renyu Duan,Z. Li,Zhihao Kong,Liwen Zhang,Lei Dai,Yanfei Wang,Qingjie Sun,David Julian McClements,Caili Wang,Xingfeng Xu
出处
期刊:Food Hydrocolloids [Elsevier BV]
卷期号:148: 109436-109436 被引量:36
标识
DOI:10.1016/j.foodhyd.2023.109436
摘要

This study investigated the impact of non-covalent interactions of pea protein isolate (PPI), quillaja saponin (QS) and tannic acid (TA) on the physiochemical, interfacial, and emulsifying properties of curcumin (Cur)-loaded composite nanoparticles from microscopic to macroscopic scales. Hydrogen bonding was important for all the nanoparticles, while hydrophobic interaction was also the dominate driving force to maintain internal structure of Cur/PPI and Cur/PPI-QS 2:1 nanoparticle. The presence of TA decreased the particle size but increased the encapsulation efficiency of Cur. The encapsulation efficiency of Cur/PPI and TA-Cur/PPI were 49.7% and 74.7%, respectively. The thermal and light stability of Cur were enhanced with the addition of TA. X-ray Diffraction result verified that Cur was successfully captured into composite nanoparticles in an amorphous state. Both of Cur/PPI-QS 2:1 and TA-Cur/PPI-QS 2:1 exhibited relative lower interfacial tension (6.3 and 5.2 mN/m, respectively) and the near-neutral wettability (74.5°and 88.1°, respectively), indicating their stronger interfacial adsorption capability. Quartz crystal microbalance with dissipation (QCM-D) analyses confirmed that TA-Cur/PPI-QS 2:1 showed more viscoelasticity interfacial film with highest K4 (0.179 × 10−6 Hz). Furthermore, the TA-Cur/PPI-QS 2:1 Pickering emulsion exhibited solid-like behavior and stronger gel network structure. Both of TA-Cur/PPI-QS 2:1- and Cur/PPI-QS 2:1-stabilized Pickering emulsions showed better storage stability than other samples. This study presents a practical strategy for the structural design of protein nanoparticles by tuning non-covalent interactions, and provides theoretical support for multi-scale exploration of structure-properties relationships of nanoparticle.
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