Binding of β-carotene to whey proteins: Multi-spectroscopic techniques and docking studies.
Circular dichroism
Docking study
Fluorescence quenching
Thermodynamic parameters
Whey protein isolate
β-Carotene
Journal
Food chemistry
ISSN: 1873-7072
Titre abrégé: Food Chem
Pays: England
ID NLM: 7702639
Informations de publication
Date de publication:
30 Mar 2019
30 Mar 2019
Historique:
received:
16
05
2018
revised:
10
10
2018
accepted:
10
10
2018
entrez:
4
12
2018
pubmed:
7
12
2018
medline:
19
1
2019
Statut:
ppublish
Résumé
The objective of this work was to study molecular binding between β-carotene (β-C) and whey protein isolate (WPI) as a function of pH (4-9), temperature (15, 25, and 35 °C), and NaCl concentration (0-0.25 M) using spectroscopic techniques and docking studies. The fluorescence quenching data showed that binding affinity increased with pH, temperature and ionic strength. The binding was entropy driven and involved mostly hydrophobic interactions. Three major whey proteins including β-lactoglobulin (β-Lg), α-lactalbumin (α-Lac), and bovine serum albumin (BSA) were bound to β-C with overall binding constant values of 1.31 × 10
Identifiants
pubmed: 30502216
pii: S0308-8146(18)31822-3
doi: 10.1016/j.foodchem.2018.10.057
pii:
doi:
Substances chimiques
Whey Proteins
0
beta Carotene
01YAE03M7J
Sodium Chloride
451W47IQ8X
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
96-106Informations de copyright
Copyright © 2018 Elsevier Ltd. All rights reserved.