ArticleFood chemistry. Molecular sciences2025
Glutathione as a taste modulator: molecular mechanisms of interaction with umami and sweet taste receptors.
Article in Food chemistry. Molecular sciences, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Comprehensive Taste Profile Assessment of Underexplored Amino Acids and Protein Derivatives in Umami and Koku.Foods (Basel, Switzerland) · 2026Article
- Generation of Koku-Related Peptides Using Gamma-Glutamyl Transpeptidase Post-Treatment in Porcine Liver Hydrolyzates.International journal of molecular sciences · 2026Article
- Sweet and umami TAS1R receptors: from molecular recognition to physiological function.Chemical senses · 2026Review
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Reduced L-glutathione (GSH) is a kokumi active tripeptide that enhances umami, salty, and sweet taste perceptions, probably via the calcium-sensing receptor (CaSR). In this study, we report that GSH is a partial agonist of the umami taste receptor (hTAS1R1/rTAS1R3). Using cellular assays, we revealed synergistic effects of GSH with L-glutamic acid (L-Glu) but not with 5'-ribonucleotides. Combining molecular modeling and mutagenesis studies, we mapped the GSH binding site located between the two lobes of the Venus Flytrap domain (VFT) of hTAS1R1. Interestingly, GSH is a weak agonist of the sweet taste receptor (hTAS1R2/hTAS1R3) and synergizes with sucralose via the rTAS1R3 subunit. Using the chimeric TAS1R3 receptor and site-directed mutagenesis, we showed that GSH binds to TAS1R3-VFT. This research provides increased understanding of the molecular interactions between GSH and TAS1Rs and suggests that the kokumi activity of GSH is more complex than affecting CaSR alone.
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