Individual Maillard reaction products (MRPs), namely, free and protein-bound glycated amino acids as well as dicarbonyl compounds, were quantitated in various types of brewing malt using chromatographic means. Among the protein-bound glycated amino acids, which were analyzed following enzymatic hydrolysis, N-epsilon-fructosyllysine was the dominating compound in light (EBC < 10) and dark (10 < EBC < 500) malts, accounting for up to 15.9% of lysine derivatization, followed by N-epsilon-maltulosyllysine (light malts, up to 4.9% lysine derivatization) or pyrraline (dark malts, up to 10.4% lysine derivatization). Roasting of malt led to the degradation of most of the protein-bound glycated amino acids. The same trends were visible for free glycated amino acids. A novel MRP-derived Strecker aldehyde, namely, 5-(2'-formyl-5'-hydroxymethylpyrrol-1'-yl)-pentanal (pyrralinal), was detected in dark malt. The most abundant 1,2-dicarbonyl compound in malt samples was 3-deoxyglucosone (up to 9 mmol/kg), followed by 3-deoxymaltosone (up to 2 mmol/kg). Only few MRPs such as 5-hydroxymethylfurfural, furfural, the dicarbonyl compounds glyoxal, methylglyoxal, and diacetyl as well as protein-bound rhamnolysine and MG-H1 correlated with the malt color. A comparison of MRPs present in malt with corresponding amounts in beer points to neoformation of MRPs such as MG-H1 and 3-deoxygalactosone during the brewing process.