Preparation and Structural Characterization of Pea Protein-Curcumin Nanoparticles by pH-Driven Method
CSTR:
Author:
Affiliation:

(1.Beijing Engineering Research Center of Protein and Functional Peptides, China National Research Institute of Food and Fermentation Industries, Beijing 100015;2.Department of Environment and Life Sciences, Beijing University of Technology, Beijing 100124;3.College of Food Science and Engineering, Beijing University of Agriculture, Beijing 100096;4.College of Engineering, China Agricultural University, Beijing 100083)

Clc Number:

Fund Project:

  • Article
  • |
  • Figures
  • |
  • Metrics
  • |
  • Reference
  • |
  • Related
  • |
  • Cited by
  • |
  • Materials
  • |
  • Comments
    Abstract:

    The poor water solubility and instability of curcumin hinders its widespread application. The use of plant proteins as delivery vehicles for curcumin can effectively improve its solubility and stability. A pH-controlled method was used to realise the nanoencapsulation of curcumin using pea protein (PPI), and the effects of pH combination, quality concentration of curcumin and quality concentration of pea protein on the loading rate of pea protein-curcumin nanoparticles were investigated by one-way experiments. Taking the loading efficiency and loading amount as indicators, the preparation process of PPI-curcumin nanoparticles was optimised by response surface methodology experiments, and the optimal preparation process of PPI-curcumin nanoparticles was obtained, i.e. the pH combinations of pH 13 and pH 8, the mass concentration of curcumin at 0.455 mg/mL, and the mass concentration of pea protein at 43.64 mg/mL. The PPI-Cur nanoparticles prepared by the optimal process were then systematically characterized in terms of particle size, ζ-potential, appearance and morphology, UV spectra and secondary structure changes. The results showed that the average particle size of the PPI-Cur nanoparticles was (254.5±9.0) nm, the ζ-potential was (-39.7±0.14) mV, the PPI-Cur nanoparticle system was stable, and the complex interaction between curcumin and pea protein complexation existed, and the secondary structure of PPI-Cur nanoparticles changed, with a significant decrease in β-folding from 33.6% to 25% (P < 0.05) and a significant increase in random curling from 23% to 31% (P < 0.05). The results provide an optimal process for the preparation of PPI-Cur nanocomplexes by pH-driven methods and a parametric basis for the development and application of plant protein-based delivery systems.

    Reference
    Related
    Cited by
Get Citation
Share
Article Metrics
  • Abstract:
  • PDF:
  • HTML:
  • Cited by:
History
  • Received:October 11,2023
  • Revised:
  • Adopted:
  • Online: December 16,2024
  • Published:
Article QR Code
Copyright :Journal of Chinese Institute of Food Science and Technology     京ICP备09084417号-4
Address :9/F, No. 8 North 3rd Street, Fucheng Road, Haidian District, Beijing, China      Postal code :100048
Telephone :010-65223596 65265376      E-mail :chinaspxb@vip.163.com
Supported by : Beijing E-Tiller Technology Development Co., Ltd.