Heating of milk and dairy products is done using various technological processes with the aim of preserving microbiological safety and extending shelf-life. These treatments result in chemical modifications in milk proteins, mainly generated as a result of the Maillard reaction. Recently, different bottom-up proteomic methods have been applied to characterize the nature of these structural changes and the modified amino acids in model protein systems and/or isolated components from thermally-treated milk samples. On the other hand, different gel-based and shotgun proteomic methods have been utilized to assign glycation, oxidation and glycoxidation protein targets in diverse heated milks. These data are essential to rationalize eventual, different nutritional, antimicrobial, cell stimulative and antigenic properties of milk products, because humans ingest large quantities of corresponding thermally modified proteins on a daily basis and these molecules also occur in pharmaceuticals and cosmetics. This review provides an updated picture of the procedures developed for the proteomic characterization of variably-heated milk products, highlighting their limits as result of concomitant factors, such as the multiplicity and the different concentration of the compounds to be detected.
Keywords: Advanced-glycation end-products; Furosine (CID 123889); Glyoxal (CID 7860); Heating; Lactose (CID 440995); Lactosylation; Lactulosyl-l-lysine (CID 3082392); Maillard reaction; Methylglyoxal (CID 880); Milk; N(ε)-carboxyethyl-l-lysine (CID 11241427); N(ε)-carboxymethyl-l-lysine (CID 123800); N-formyl-l-kynurenine (CID 910); Oxidation; Pentosidine (CID 119593); l-Methionine sulfoxide (CID 158980).
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