Characterization of the binding of cyanidin-3-glucoside to bovine serum albumin and its stability in a beverage model system: A multispectroscopic and chemometrics study.
Animals
Anthocyanins
/ chemistry
Beverages
Binding Sites
Calorimetry, Differential Scanning
Cattle
Circular Dichroism
Glucosides
/ chemistry
Hydrogen Bonding
Hydrogen Peroxide
/ metabolism
Microscopy, Atomic Force
Models, Molecular
Models, Structural
Oxidation-Reduction
Protein Binding
Serum Albumin, Bovine
/ chemistry
Spectrometry, Fluorescence
Temperature
Anthocyanin
Bovine serum albumin
Chemometrics
Interaction
Stabilization
Journal
Food chemistry
ISSN: 1873-7072
Titre abrégé: Food Chem
Pays: England
ID NLM: 7702639
Informations de publication
Date de publication:
01 May 2020
01 May 2020
Historique:
received:
03
06
2019
revised:
30
11
2019
accepted:
03
12
2019
pubmed:
22
12
2019
medline:
14
4
2020
entrez:
22
12
2019
Statut:
ppublish
Résumé
Anthocyanins as one of the main natural groups of food colorants undergo quick color fading, which can be diminished through protein association. The stabilization of cyanidin-3-glucoside (CYG) through binding to bovine serum albumin (BSA) was investigated at pH 3.0 using atomic force microscopy and differential scanning calorimetry along with UV-Vis absorption, steady-state fluorescence, circular dichroism, and three-dimensional emission spectral analyses merged with the multivariate curve resolution-alternative least square method. The stabilized CYG molecules were found at the site II of BSA with combined static and dynamic quenching mechanisms. Approximately 93% of the BSA binding sites were occupied in the BSA-CYG complex through hydrogen bonds and van der Waals forces with the binding constant and stoichiometry ratio of 1.88 × 10
Identifiants
pubmed: 31864188
pii: S0308-8146(19)32158-2
doi: 10.1016/j.foodchem.2019.126015
pii:
doi:
Substances chimiques
Anthocyanins
0
Glucosides
0
cyanidin-3-O-beta-glucopyranoside
0
Serum Albumin, Bovine
27432CM55Q
Hydrogen Peroxide
BBX060AN9V
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
126015Informations de copyright
Copyright © 2019 Elsevier Ltd. All rights reserved.