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pH-Dependent complexation between β-lactoglobulin and lycopene: Multi-spectroscopy, molecular docking and dynamic simulation study
- Source :
- Food chemistry. 362
- Publication Year :
- 2021
-
Abstract
- This study aims to investigate the effect of pH levels (pH 7.0 and pH 8.1) on binding ability of β-lactoglobulin (β-LG) with lycopene (LYC) and elucidate interaction mechanisms using multi-spectroscopy and molecular docking study. β-LG at pH 8.1 showed a stronger binding affinity to lycopene than that at pH 7.0 according to binding constant, binding number, energy transfer efficiency, and surface hydrophobicity. Lycopene bound to protein mainly by van der Waals force in the form of static quenching mode and preferred to interact with β-LG at the top of barrel for both pH levels. Molecular dynamic simulation revealed that β-LG/LYC complex at pH 8.1 was more stable than at pH 7.0. β-LG/LYC complexes formed at pH 8.1 showed significantly higher ABTS radical scavenging activity than samples at pH 7.0 (p 0.05). Data obtained may contribute valuable information for preparing a whey protein-based delivery system for lycopene.
- Subjects :
- Ph dependent
Lactoglobulins
Molecular Dynamics Simulation
01 natural sciences
Analytical Chemistry
chemistry.chemical_compound
symbols.namesake
Molecular dynamics
0404 agricultural biotechnology
Lycopene
Spectroscopy
ABTS
Quenching (fluorescence)
Chemistry
Spectrum Analysis
010401 analytical chemistry
04 agricultural and veterinary sciences
General Medicine
Hydrogen-Ion Concentration
040401 food science
Binding constant
0104 chemical sciences
Molecular Docking Simulation
symbols
van der Waals force
Hydrophobic and Hydrophilic Interactions
Food Science
Nuclear chemistry
Subjects
Details
- ISSN :
- 18737072
- Volume :
- 362
- Database :
- OpenAIRE
- Journal :
- Food chemistry
- Accession number :
- edsair.doi.dedup.....992af215e5c73932c5a0e36d993db678