Background: Native walnut protein is an alkali-soluble protein that seriously limits the application of walnut protein. The pH-shifting method could improve the solubility of walnut proteins and enable the encapsulation of active ingredients. The present study aimed to prepare water-soluble nanoparticles of curcumin using walnut protein and evaluate the process of walnut protein self-assembly, interaction between walnut protein and curcumin, encapsulation properties, and stability of nanoparticles.
Results: The solubility of native walnut protein was poor, but the solubility of walnut protein nanoparticles (WPNP) formed by walnut protein after pH-shifting significantly improved to 91.5 ± 1.2%. This is because, during the process of pH changing from 7 to 12 and back to 7, walnut protein first unfolded under alkaline conditions and then refolded under pH drive, finally forming an internal hydrophobic and external hydrophilic shell-core structures. The quenching type of walnut protein and curcumin was static quenching, and the quenching constant was 2.0 × 10 mol L s , indicating that the interaction between walnut protein and curcumin was non-covalent. Adding curcumin resulted in the formation of nanoparticles with small particle size compared with the no-load. The loading capacity of curcumin-loaded walnut protein nanoparticles (WPNP-C) was 222 mg g walnut protein isolate. Under the same mass, the curcumin equivalent concentration in aqueous solution of WPNP-C was 17 000 times higher than that of the native curcumin.
Conclusion: The solubility of the self-assembled WPNP significantly increased after pH-shifting treatment. The walnut protein carrier could improve the stability of the encapsulated curcumin. Therefore, walnut proteins could be used as water-soluble carriers for hydrophobic drugs. © 2023 Society of Chemical Industry.
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http://dx.doi.org/10.1002/jsfa.12559 | DOI Listing |
J Allergy Clin Immunol Pract
January 2025
Institute of Allergy, Immunology and Pediatric Pulmonology, Yitzhak Shamir Medical Center; Department of Pediatrics, Faculty of Medicine, Tel Aviv University.
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Food Chem
January 2025
State Key Laboratory for Food Nutrition and Safety; College of Food Science and Engineering, Tianjin University of Science and Technology, Tianjin 300457, China. Electronic address:
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Department of Nutrition and Movement Sciences, NUTRIM Institute of Nutrition and Translational Research in Metabolism, Maastricht University Medical Center, 6229 ER Maastricht, The Netherlands.
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Foods
January 2025
Department of Bioconvergence, Hoseo University, Asan 31499, Republic of Korea.
Alzheimer's disease (AD) prevention is a critical challenge for aging societies, necessitating the exploration of food ingredients and whole foods as potential therapeutic agents. This study aimed to identify natural compounds (NCs) with therapeutic potential in AD using an innovative bioinformatics-integrated deep neural analysis approach, combining computational predictions with molecular docking and in vitro experiments for comprehensive evaluation. We employed the bioinformatics-integrated deep neural analysis of NCs for Disease Discovery (BioDeepNat) application in the data collected from chemical databases.
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December 2024
Human-Machine Perception Laboratory, Department of Computer Science and Engineering, University of Nevada, Reno, 1664 N Virginia St, Reno, NV 89557, USA.
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