Premium
Substrate‐Driven Differences in Tryptophan Catabolism by Gut Microbiota and Aryl Hydrocarbon Receptor Activation
Author(s) -
Huang Zhan,
Schoones Tessa,
Wells Jerry M.,
Fogliano Vincenzo,
Capuano Edoardo
Publication year - 2021
Publication title -
molecular nutrition and food research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.495
H-Index - 131
eISSN - 1613-4133
pISSN - 1613-4125
DOI - 10.1002/mnfr.202100092
Subject(s) - tryptophan , aryl hydrocarbon receptor , catabolism , biochemistry , fermentation , tryptamine , chemistry , catabolite repression , food science , amino acid , metabolism , gene , transcription factor , mutant
Scope This study aims to investigate the effect of tryptophan sources on tryptophan catabolism by gut microbiota and the aryl hydrocarbon receptor (AhR) activation. Methods and Results Four substrates (free tryptophan, soybean protein, single and clustered soybean cells) containing an equimolar amount of tryptophan, but with a different bioaccessibility are studied using in vitro batch fermentation. Tryptophan catabolites are identified by LC‐MS/MS. AhR activity is measured by HepG2‐Lucia AhR reporter cells. The total amount of tryptophan‐derived catabolites increases with decreasing level of substrate complexity. Indole is the major catabolite produced from tryptophan and it is the most abundant in the free tryptophan fermentation. Indole‐3‐acetic acid and indole‐3‐aldehyde are abundantly generated in the soybean protein fermentation. The soybean cell fermentation produced high concentrations of tryptamine. Interestingly, large amounts of short‐chain fatty acids (SCFAs) are also found in the soybean cell and protein fermentation. Both tryptophan‐derived catabolites and SCFAs are able to increase AhR reporter activity over time in all four groups. Conclusion This study illustrates that bacterial catabolism of tryptophan and resulting AhR activation in the gut is modulated by the food matrix, suggesting a role for food design to improve gut health.