Tangeretin-loaded protein nanoparticles fabricated from zein/β-lactoglobulin: Preparation, characterization, and functional performance

• Published in: Food chemistry Vol. 158; pp. 466 - 472
• Main Authors: Chen, Jingjing, Zheng, Jinkai, McClements, David Julian, Xiao, Hang
• Format: Journal Article
• Language: English
• Published: Kidlington Elsevier Ltd 01.09.2014; Elsevier
• Subjects: Agglomeration; Biological and medical sciences; Colloids; Drug Carriers - chemistry; Drug Delivery Systems; Encapsulation; Flavones - chemistry; Food toxicology; Foods; Freeze Drying; Hydrogen-Ion Concentration; Lactoglobulins - chemistry; Medical sciences; Nanoparticles; Nanoparticles - chemistry; Nutraceuticals; Osmolar Concentration; Particle Size; Proteins; Solubility; Static Electricity; Tangeretin; Temperature; Toxicology; Zein; Zein - chemistry; β-Lactoglobulin; Nanoparticles; Zein; β-Lactoglobulin; Tangeretin; Solubility; Nutraceuticals; Characterization; Performance evaluation; Functional; Ultrafine particle; Performance; Protein
• ISSN: 0308-8146; 1873-7072
• DOI: 10.1016/j.foodchem.2014.03.003

•Tangeretin-loaded protein nanoparticles were produced.•The particles can be readily dispersed in aqueous food products.•The influence of environment factors on nanoparticles stability was established. The aim of this study was to design a colloidal delivery system to encapsulate poor water-soluble bioactive flavonoid tangeretin so that it could be utilized in various food products as functional ingredient. Tangeretin-loaded protein nanoparticles were produced by mixing an organic phase containing zein and tangeretin with an aqueous phase containing β-lactoglobulin and then converted into powder by freeze-drying. This powder formed a colloidal suspension when dispersed in water that is relatively stable to particle aggregation and sedimentation. The influence of temperature, ionic strength, and pH on the stability of the protein nanoparticles was tested. Extensive particle aggregation occurred at high ionic strength (>100mM) and intermediate pH (4.5–5.5) due to reduced electrostatic repulsion. Extensive aggregation also occurred at temperatures exceeding 60°C, which was presumably due to increased hydrophobic attraction. Overall, this study shows that protein-based nanoparticles can be used to encapsulate bioactive tangeretin so that it can be readily dispersed in compatible food products.