Generation of advanced glycation end products from glycated protein or fructose/glyoxal-protein adducts under in vitro simulated gastrointestinal digestion.
Advanced glycation end products
Digestion
Fructose
Maillard reaction
Nε-carboxymethyllysine
α-Dicarbonyls compounds
Journal
Food chemistry
ISSN: 1873-7072
Titre abrégé: Food Chem
Pays: England
ID NLM: 7702639
Informations de publication
Date de publication:
07 Sep 2024
07 Sep 2024
Historique:
received:
07
02
2024
revised:
08
07
2024
accepted:
05
09
2024
medline:
16
9
2024
pubmed:
16
9
2024
entrez:
15
9
2024
Statut:
aheadofprint
Résumé
Advanced glycation end products (AGEs) are a heterogeneous group of compounds formed both endogenously and exogenously through reactions between reducing sugars and amino acids within the proteins. The digestive tract may also serve as a site for endogenous AGEs generation. This study examined whether additional AGEs are formed during the digestion of glycated protein diets and meal-resembling systems (dietary proteins with fructose or glyoxal). The digestion of glycated protein showed that free AGEs were gradually released, but no additional AGEs were generated. In contrast, co-digestion of dietary proteins with fructose or glyoxal resulted in the formation of additional AGEs, and the reaction substrates (fructose or glyoxal) were depleted during digestion. Additionally, the lysine released from proteins decreased, leading to a loss of nutritional value of the food during co-digestion. The formation of AGEs and the depletion of essential amino acids in the gut may have significant implications for human health.
Identifiants
pubmed: 39278073
pii: S0308-8146(24)02825-5
doi: 10.1016/j.foodchem.2024.141175
pii:
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
141175Informations de copyright
Copyright © 2024. Published by Elsevier Ltd.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare no competing financial interests.