Preparation and Stability Characterization of Burdock Root Protein-antihypertensive Peptide Nanoparticles
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Abstract:
In this study, burdock root protein (BRP) was obtained by buffer extraction, and burdock root protein nanoparticles (BANPs) loaded with loach antihypertensive peptide (Alanine-Histidine-Leucine-Leucine, AHLL) were then prepared. BANPs were formed by BRP and AHLL via self-assembly. The structure and intermolecular interactions of BANPs were studied by scanning electron microscopy, fluorescence and UV-Vis spectroscopy, and Fourier transform infrared spectroscopy. The stability of BANPs under different temperatures and pHs was also investigated. The results showed that the BANPs had a smaller particle size (231.47 nm) and negative charge (-19.10 mV), and were formed through electrostatic and hydrophobic interactions between BRP and AHLL at pH 5. As the mass concentrations of BRP and AHLL increased, the AHLL encapsulation efficiency increased and drug loading content increased (to 77.28% and 23.90%, respectively when BRP=8 mg/mL and AHLL=200 μg/mL). The BANPs showed a high stability in the temperature range of 60~100 ℃ and pH range of 4.0~8.0. Compared to free AHLL, the degradation rate of encapsulated AHLL was as low as 33.16%. This study has shown that BRP nanocarriers can effectively protect AHLL against the impacts of pH and thermal degradation, thus have the potential as a nano-delivery system for bioactive peptides in functional foods.
