pH-Dependent complexation between ß-lactoglobulin and lycopene: Multi-spectroscopy, molecular docking and dynamic simulation study.
Food Chem
; 362: 130230, 2021 Nov 15.
Article
em En
| MEDLINE
| ID: mdl-34098435
ABSTRACT
This study aims to investigate the effect of pH levels (pH 7.0 and pH 8.1) on binding ability of ß-lactoglobulin (ß-LG) with lycopene (LYC) and elucidate interaction mechanisms using multi-spectroscopy and molecular docking study. ß-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 ß-LG at the top of barrel for both pH levels. Molecular dynamic simulation revealed that ß-LG/LYC complex at pH 8.1 was more stable than at pH 7.0. ß-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.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Análise Espectral
/
Simulação de Dinâmica Molecular
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Simulação de Acoplamento Molecular
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Licopeno
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Lactoglobulinas
Idioma:
En
Revista:
Food Chem
Ano de publicação:
2021
Tipo de documento:
Article
País de afiliação:
China