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Organic compounds with conjugated double bonds show strong absorption features in the UV–visible region of the electromagnetic spectrum attributed to π → π* electronic excitations. Generally, a UV–vis absorption spectrum is recorded as a plot of absorbance vs wavelength. The wavelength of maximum absorbance, which manifests as a peak in the absorption spectrum, is denoted as λmax.
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pH-Dependent complexation between β-lactoglobulin and lycopene: Multi-spectroscopy, molecular docking and dynamic

Ce Wang1, Lu Chen1, Yingcong Lu1

  • 1Department of Food Science, College of Food Science and Engineering, Jilin University, Changchun 130062, China.

Food Chemistry
|June 7, 2021
PubMed
Summary
This summary is machine-generated.

Higher pH (8.1) enhances beta-lactoglobulin (β-LG) binding with lycopene (LYC), improving its stability and antioxidant activity. This suggests potential for whey protein delivery systems.

Keywords:
Dynamic simulation studyLycopeneMolecular dockingSpectroscopic analysisβ-lactoglobulin

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Area of Science:

  • Food Science
  • Biochemistry
  • Protein Chemistry

Background:

  • Beta-lactoglobulin (β-LG) is a major whey protein with potential applications in nutrient delivery.
  • Lycopene (LYC) is a potent antioxidant with poor bioavailability.
  • Understanding protein-carotenoid interactions is crucial for developing effective delivery systems.

Purpose of the Study:

  • To investigate the impact of pH (7.0 vs. 8.1) on β-LG/LYC binding.
  • To elucidate the molecular mechanisms governing this interaction.
  • To assess the effect of pH on the antioxidant capacity of β-LG/LYC complexes.

Main Methods:

  • Multi-spectroscopy techniques (fluorescence, UV-Vis absorption).
  • Molecular docking and dynamic simulations.
  • Binding constant and thermodynamic parameter determination.
  • ABTS radical scavenging assay.

Main Results:

  • β-LG exhibited stronger binding affinity for LYC at pH 8.1 compared to pH 7.0.
  • Interactions were primarily driven by van der Waals forces via static quenching.
  • Molecular dynamics confirmed greater stability of the β-LG/LYC complex at pH 8.1.
  • Complexes formed at pH 8.1 demonstrated significantly enhanced ABTS radical scavenging activity.

Conclusions:

  • pH significantly influences the binding interaction and stability of β-LG/LYC complexes.
  • The enhanced binding and stability at pH 8.1 lead to improved antioxidant properties.
  • Findings support the use of whey protein, specifically β-LG, as a delivery vehicle for lycopene.