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Published on: April 13, 2019
Protein-bound and free glycation compounds in human milk: A comparative study with minimally processed infant formula
Simona Arena1, Sabrina De Pascale1, Valentina Ciaravolo1
1Proteomics, Metabolomics and Mass Spectrometry Laboratory, Institute for the Animal Production System in the Mediterranean Environment, National Research Council (ISPAAM-CNR), Portici, Italy.
Abstract:
The role of the Maillard reaction and the accumulation of non-enzymatic glycation compounds in human milk have been scarcely considered. In this study, we investigated the proteins most susceptible to glycation, the identity of the corresponding modified residues and the quantitative relationship between protein-bound and free glycation compounds in raw human milk and, for comparison, in minimally processed infant formula and pasteurized bovine milk. In human milk, total protein-bound lysine modifications were up to 10% of the counterparts in infant formula, while Nε-carboxymethyllysine reached up to 27% of the concentration in the other two products. We demonstrated that the concentration of free pyrraline and methylglyoxal-hydroimidazolone were of the same order of magnitude in the three milk types. Our results delineate how the occurrence of some glycation compounds in human milk can be an unavoidable part of the breastfeeding and not an exclusive attribute of infant formulas and pasteurized bovine milk.
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