Loading performance of micellar casein-pectin composite microcapsules for emodin

  • YANG Min ,
  • WA Wenqiang ,
  • LIANG Huiguang ,
  • JI Wei ,
  • LI Qian
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  • (College of Science, Gansu Agricultural University, Lanzhou 730070, China)

Received date: 2023-05-05

  Revised date: 2023-06-09

  Online published: 2024-07-11

Abstract

Emodin (E), the main active ingredient in rhubarb, is a hydrophobic molecule.Micellar casein (MC) is the natural state of caseins in milk.In this study, the interaction between MC and E was calculated by fluorescence analysis with the addition of pectin (P).The average size and structure of P-MC@E complexes were analyzed, as well as their DPPH free radical and ABTS cationic radical scavenging activities.In addition, the release profiles of emodin from the complexes were evaluated by a simulated gastrointestinal digestion experiment.Results showed that the major interaction between MC and emodin was hydrophobic forces in the P-MC system with the ratio of P to MC in the range of 0∶10-5∶5, the binding constant of which was greater than 103.With the increase of pectin content, the particle size of P-MC@E complexes increased gradually, but its infrared spectra did not change significantly.Furthermore, the DPPH free radical and ABTS cationic radical scavenging activities of the complexes were significantly higher than those of free emodin, which increased with the increase of pectin content.After binding with P-MC, the release rate of emodin during simulated gastrointestinal digestion decreased.The results could provide basic references for the loading and delivery of emodin.

Cite this article

YANG Min , WA Wenqiang , LIANG Huiguang , JI Wei , LI Qian . Loading performance of micellar casein-pectin composite microcapsules for emodin[J]. Food and Fermentation Industries, 2024 , 50(12) : 24 -31 . DOI: 10.13995/j.cnki.11-1802/ts.036025

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