Abstract
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-ε-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-ε-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 comp...Continue Reading
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Citations
Jun 4, 2021·Journal of Agricultural and Food Chemistry·Tomás Herraiz, Fernando Vera
Aug 7, 2021·Scientific Reports·Edward D KerrBenjamin L Schulz
Oct 22, 2021·Journal of Agricultural and Food Chemistry·Michael HellwigThomas Henle