Protein-bound and free glycation compounds in human milk: A comparative study with minimally processed infant formula and pasteurized bovine milk

Publication date

2025-01-15

Authors

Arena, Simona
De Pascale, Sabrina
Ciaravolo, Valentina
Monroy, Mariela Mejia
Gouw, J.W.ISNI 0000000396050784
Stahl, BerndISNI 0000000527564962
Bäuerl, Christine
Collado, Maria Carmen
De Filippo, Carlotta
Scaloni, Andrea

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Advisors

Supervisors

Document Type

Article
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cc_by

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.

Keywords

Human milk, Infant formula, Maillard reaction, Mass spectrometry, Analytical Chemistry, Food Science

Citation

Arena, S, De Pascale, S, Ciaravolo, V, Monroy, M M, Gouw, J W, Stahl, B, Bäuerl, C, Collado, M C, De Filippo, C, Scaloni, A & Troise, A D 2025, 'Protein-bound and free glycation compounds in human milk : A comparative study with minimally processed infant formula and pasteurized bovine milk', Food Chemistry, vol. 463, no. Pt 2, 141265. https://doi.org/10.1016/j.foodchem.2024.141265