Adducts Derived from (-)-Epigallocatechin Gallate-Amadori Rearrangement Products in Aqueous Reaction Systems: Characterization, Formation, and Thermolysis

The interaction mechanism of (-)-epigallocatechin gallate (EGCG) with Amadori compound (Amadori rearrangement product, ARP) in xylose-alanine model reaction systems was investigated. The adducts between ARP and EGCG were identified as two ARP-EGCG isomers, two ARP-EGCG-H2O isomers, and multiple ARP-deoxypentosone (DP)-EGCG isomers. The structure of an isolated and purified ARP-EGCG adduct was analyzed by means of Fourier transform infrared spectroscopy, ultraviolet-visible spectroscopy, liquid chromatography-time-of-flight (TOF)-mass spectrometry (LC-TOF-MS), and nuclear magnetic resonance (NMR). Using the two-dimensional NMR analyses, the structure of ARP-EGCG adducts was clarified to consist of a covalent linkage between the C-12 position of the ARP and the C-8 position of the A-ring of EGCG, presumably generated by the nucleophilic nature of the EGCG or aromatic substitution reactions. The results showed that slightly alkaline pH and higher temperature could facilitate this reaction. Additionally, the thermal stability of ARP-EGCG and its degradation products revealed that the decomposition pathways of this adduct altered the classic decomposition pathway of ARP, resulting in a lower browning rate and blocking the subsequent Maillard reaction.