PH-Dependent complexation between β-lactoglobulin and lycopene: Multi-spectroscopy, molecular docking and dynamic simulation study. (15th November 2021)

• Record Type: Journal Article
• Authors: Wang, Ce; Chen, Lu; Lu, Yingcong; Liu, Jia; Zhao, Ru; Sun, Yonghai; Sun, Boyang; Cuina, Wang
• Is Part Of: Food chemistry. Volume 362(2021)
• Publication Date: 2021-11-15
• Subjects: Lycopene -- β-lactoglobulin -- Spectroscopic analysis -- Molecular docking -- Dynamic simulation study; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2021.130230
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: pH 8.1 was more beneficial to complexation between β-LG and lycopene. LYC lies on top of β-LG barrel predominantly via van der Waals force at both pH. β-LG/LYC complexes at pH 8.1 was more stable than at pH 7.0. 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.