Interactions between polyphenol oxidation products and salivary proteins: Specific affinity of CQA dehydrodimers with cystatins and P-B peptide.
Apple juice
Astringency
Chlorogenic acid
Human saliva
Polyphenols
Journal
Food chemistry
ISSN: 1873-7072
Titre abrégé: Food Chem
Pays: England
ID NLM: 7702639
Informations de publication
Date de publication:
01 May 2021
01 May 2021
Historique:
received:
07
07
2020
revised:
23
10
2020
accepted:
25
10
2020
pubmed:
19
11
2020
medline:
15
1
2021
entrez:
18
11
2020
Statut:
ppublish
Résumé
Throughout the apple juice and cider making process, polyphenols undergo enzymatic oxidation which generates a great variety of polyphenol oxidation products. Since 5'-O-Caffeoylquinic acid (CQA) is one of the major phenolic compounds and the preferential substrate for polyphenoloxidase in apple juice, its oxidation leads to the formation of newly formed molecules by which dehydrodimers (MW 706 Da) are included. Interactions of salivary proteins (SP) with native polyphenols is a well-known phenomenon, but their interactions with polyphenol oxidation products has not been studied yet. In this work, we decided to decipher the interactions between CQA dehydrodimers and SP (gPRPs, aPRPs, statherins/P-B peptide, and cystatins) using HPLC-UV and fluorescence. These results showed that contrary to what was expected, CQA dehydrodimers presented a low interaction with PRPs, but revealed a specific interaction with statherins/P-B peptide and cystatins. This work settles for the first time the interactions between SP and polyphenol oxidation products.
Identifiants
pubmed: 33203598
pii: S0308-8146(20)32358-X
doi: 10.1016/j.foodchem.2020.128496
pii:
doi:
Substances chimiques
Cystatins
0
Polyphenols
0
Salivary Proteins and Peptides
0
caffeoylquinic acid
0
Quinic Acid
058C04BGYI
Catechol Oxidase
EC 1.10.3.1
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
128496Informations de copyright
Copyright © 2020 Elsevier Ltd. All rights reserved.