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Interactions between puerarin/daidzein and micellar casein
Yucheng Wang1, Min Yang1, Juanjuan Qin1
1College of Science, Gansu Agricultural University, Lanzhou, China.
Micellar casein enhances the bioavailability of puerarin (PUE) and daidzein (DAI) by forming complexes that prolong their release during digestion. This improves their antioxidant activity and potential for food and pharmaceutical applications.
Area of Science:
- Food Chemistry
- Biochemistry
- Materials Science
Background:
- Puerarin (PUE) and daidzein (DAI) are bioactive polyphenols with limited solubility and bioavailability.
- Micellar casein (MC) is a protein with potential for encapsulating and improving the delivery of bioactive compounds.
Purpose of the Study:
- To investigate the interactions between PUE/DAI and MC.
- To analyze the physicochemical properties of PUE-MC and DAI-MC complexes.
- To evaluate the impact of complexation on antioxidant activity and in vitro release.
Main Methods:
- Fluorescence spectroscopy
- Molecular docking
- FTIR and XRD analyses
- DPPH radical scavenging assay
- In vitro release studies
Main Results:
- Complexes formed between MC and PUE/DAI via hydrogen bonding (PUE-MC) and hydrophobic forces (DAI-MC).
- Complexation increased MC size and decreased its weight loss rate, without significant morphological changes.
- PUE-MC and DAI-MC complexes exhibited enhanced DPPH radical scavenging capacity compared to free PUE/DAI.
- MC encapsulation inhibited the in vitro release rate of PUE and DAI under simulated intestinal conditions.
Conclusions:
- Micellar casein effectively complexes with PUE and DAI, improving their physicochemical properties.
- Complexation enhances antioxidant activity and prolongs the release of PUE and DAI, boosting bioavailability.
- These findings support the use of MC for developing PUE and DAI delivery systems in food and pharmaceuticals.
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