期刊
FOOD RESEARCH INTERNATIONAL
卷 161, 期 -, 页码 -出版社
ELSEVIER
DOI: 10.1016/j.foodres.2022.111870
关键词
Myofibrillar protein-bound N-epsilon-(carboxymethyl) lysine; Simulated gastrointestinal digestion; Absorption; Transport; Caco-2 cell
资金
- National Natural Science Foundation of China [31901788, 32172317]
- Postdoctoral Science Foundation of China [2018M633586]
- Doctoral Fund of Shaanxi Province [F2020221004]
This study aimed to investigate the absorption and transport of myofibrillar protein-bound N epsilon-(carboxymethyl) lysine (MP-bound CML) in Caco-2 cells after simulated gastrointestinal digestion. The results showed that MP-bound CML can be absorbed by Caco-2 cells and transported across the cell barrier through different pathways.
This study aimed to investigate the absorption and transport of myofibrillar protein-bound N epsilon-(carboxymethyl) lysine (MP-bound CML) in Caco-2 cells after simulated gastrointestinal digestion. Four kinds of MP-bound CML hydrolysates with molecular weights (MWs) less than 1 kDa, 1-3 kDa, 3-5 kDa and greater than 5 kDa, were obtained by ultrafiltration; their absorption and transport were studied in Caco-2 cells. Peptide-bound CML in hydrolysates with MWs less than 1 kDa was absorbed by 6.58 % and might transport across Caco-2 cells monolayer through paracellular pathway; peptide-bound CML in hydrolysates with MWs 1-3 kDa was absorbed by 12.8 % and might transport across Caco-2 cells monolayer through paracellular pathway and transcytosis route; peptide-bound CML in hydrolysates with MWs 3-5 kDa was absorbed by 14.66 % and might be through active route via PepT-1 transport across Caco-2 cells monolayer; whereas protein-bound CML in hydrolysates with MWs greater than 5 kDa was only absorbed by 1.02 %, which was hardly transported into Caco-2 cells. In conclusion, MP-bound CML could be absorbed by 35.06 % into Caco-2 cells after simulated gastrointestinal digestion and is transported across Caco-2 cells through paracellular pathway, transcytosis route and active route via PepT-1.
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