Pea protein based nanocarriers for lipophilic polyphenols: Spectroscopic analysis, characterization, chemical stability, antioxidant and molecular docking. (October 2022)

• Record Type: Journal Article
• Authors: Zhang, Xiaoge; Wang, Ce; Qi, Zitong; Zhao, Ru; Wang, Cuina; Zhang, Tiehua
• Is Part Of: Food research international. Volume 160(2022)
• Publication Date: 2022-10
• Subjects: Pea protein -- Curcumin -- Quercetin -- Resveratrol; Food -- Analysis -- Periodicals; Food industry and trade -- Periodicals; Food industry and trade -- Canada -- Periodicals; Food Technology -- Periodicals; Food -- Periodicals; Food-Processing Industry -- Periodicals; Aliments -- Industrie et commerce -- Périodiques; Aliments -- Industrie et commerce -- Canada -- Périodiques; Aliments -- Recherche -- Périodiques; Food industry and trade; Canada; Periodicals; Electronic journals; 664.005
• DOI: 10.1016/j.foodres.2022.111713
• Languages: English
• ISSNs: 0963-9969

Abstract

Graphical abstract: Highlights: Binding affinity of PPI towards three polyphenols declined in sequence of QUE > CUR > RES while loading capacity of RES > QUE > CUR. Thermodynamic parameters revealed the main hydrophobic interaction and hydrogen bonding were important in their assembly between CUR/QUE and RES with PPI, respectively. FTIR, XRD and DSC results verified that polyphenols changed from crystalline to amorphous state. Ultraviolet light and thermal stability, antioxidant activity of polyphenols was improved by complexation with PPI. Molecular docking indicated binding energy of legumin with three polyphenols of QUE > RES > CUR, and the binding conformation of polyphenols with its surrounding amino acids in its binding location was visualized. Abstract: The current research aims to construct and assess pea protein isolate (PPI) nanocarriers for lipophilic polyphenols of curcumin (CUR), quercetin (QUE) and resveratrol (RES), respectively. Fluorescence analysis demonstrated that the binding affinity declined in sequence of QUE > CUR > RES and about one polyphenol compound was bound to protein. Thermodynamic parameters revealed that hydrophobic interaction was mainly responsible for complexation between CUR/RES and PPI, while hydrogen bonding for QUE with PPI. All nanoparticles showed particle size of 154–159 nm. Three lipophilic polyphenols were successfully encapsulated into PPI, with loading capacity of RES > QUE > CUR. Complexation of three polyphenols did not change the secondary structure of PPI. Results of FTIR, DSC and XRD confirmed that polyphenols changed from crystalline to amorphous state after combination with PPI. SEM pictures exhibited regular spherical microstructure of nanocomplexes. PPI shielded polyphenols from sensitive environment of ultraviolet light and thermal treatment. ABTS and DPPH radical scavenging activity of polyphenols were considerably improved through complexation with PPI. Molecular docking studies showed binding energy with 11S legumin in sequence of QUE > RES > CUR, and stronger hydrogen bonds were built between QUE and the protein than the other two polyphenols. Data in the present work may provide helpful information for encapsulation of lipophilic polyphenols with pea protein and the potential application in food science, pharmaceutical and cosmetics industries in the future.