A new scientific article from our research group was published in the prestigious journal Food Chemistry with the title “Implementation of transglutaminase 2 as a crosslinking agent for salivary oral models: Effects in (in)soluble complexes formation and compound adsorption with different polyphenol families”.
In this work, the team investigated the role of the enzyme transglutaminase 2 (TGM2) as a crosslinking agent in salivary oral models. This approach enhanced the physiological relevance of the models, providing new insights into the interactions between salivary proteins and different polyphenol families. The main highlights of the work are:
- Development of a novel in vitro model mimicking oral mucosal pellicle conditions.
- Demonstration that TGM2 enhances salivary protein cross-linking to oral surfaces.
- Identification of dual astringency mechanisms: protein complexes and polyphenol adsorption.
- Characterization of tannic acid favors mucosal interaction in absence of salivary proteins.
- Specific pathway-specific analysis of polyphenol astringency mechanisms in vitro.
The study represents an important contribution to understanding the molecular mechanisms underlying sensory perceptions and the functional effects of polyphenols, which are bioactive compounds of great interest in food science and nutrition.
🔗 The full article is available online at ScienceDirect
This work was partly supported by the BeTASTy ERC Starting Grant (GA 101046462) and other funding contracts.