Studies on melanoidin-type colorants generated from the Maillard reaction of protein-bound lysine and furan-2-carboxaldehyde - Chemical characterisation of a red coloured domaine

The identification of a coloured substructure of melanoidin-type colorants is reported in the present paper. Brown-orange melanoidins with mass ≥ 10000 daltons were isolated from a thermally treated aqueous solution of casein and furan-2-carboxaldehyde using ultracentrifugation. After complete enzymatic digestion of the protein skeleton, two intense red coloured compounds were detected in the melanoidin hydrolysate by HPLC. These compounds were identified as the previously unknown chromophoric amino acid (S)-2-amino-6-{4-[(E)-1formyl-2-(2-furyl)ethenyl]-5-(2-furyl)-2-[(E)-(2- furyl) methylidene]-2,3-dihydro-3-oxo-1H-pyrrol-1-yl}hexanoic acid and its 2-[(Z)-(2-furyl)methylidene] isomer, by using several NMR techniques, by MS, UV, and IR spectroscopy. The identification of these novel compounds verifies the idea that melanoidin-type colorants can be generated by a cross-linking reaction between a low molecular weight chromophore and a non-coloured high molecular weight biopolymer.