Enterococcus faecalis : A Key Metabolic Strain of Myofibrillar Protein-Bound N ε -(Carboxymethyl)lysine In Vitro Simulated Colon after Gastrointestinal Digestion

View at publisher
Authors: Zeyu Mike Lu, Shuqi Hao, Huiqi Yan, N. N. Li, JX Hu, Wei Quan, Jiwen Cheng, H. R. Xu, Mei Li
Cited by: 1
References: 47

Abstract

Advanced glycation end products (AGEs) are consumed in massive amounts with daily diets, among which high molecular weight protein-bound AGEs, such as Myofibrillar protein-bound N ε -(carboxymethyl)lysine (MP-CML), resist gastrointestinal absorption. This study investigated MP-CML metabolism by human gut microbiota using an in vitro colonic fermentation model. MP-CML digest was separately incubated with faecal suspensions from six volunteers (F1–F3, M1–M3). The F3 sample exhibited the highest activity, reducing CML from 146.54 ± 1.45 μg/mL to 68.62 ± 2.06 μg/mL after 72 h, corresponding to a rate of 53.17%. Then, 17 potential CML-metabolizing bacteria were isolated from the fermentation broth of F3 sample. Surprisingly, strain B1, identified as Enterococcus faecalis, degraded CML at 44.1% when using MP-CML digest as the sole nutrient source. This is the first study showing that E. faecalis can metabolize protein-bound CML, which will provide new insights into the targeted regulation of CML in vivo.

Fields of Study & Subjects

Advanced Glycation End Products research Gut microbiota and health Probiotics and Fermented Foods

Publication details

Journal / source
Journal of Agricultural and Food Chemistry
Publisher
American Chemical Society (ACS)
Volume
74
Issue
1
Pages
1566–1574
Publication date
2 January 2026
Language
EN