Article in Journal

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

Arena, S., De Pascale, S., Ciaravolo, V., Monroy, M. M., Gouw, J. W., Stahl, B., ... & Troise, A. D.

Food Chemistry Volume, 2025, 462, 2, 141265

Licence: CC BY 4.0
OPEN ACCESS

September 11, 2024


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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.

This research output is related to

Spoke 06

Tackling malnutrition

To restore resilience and defeat malnutrition

Lead organisationUniPv

Spoke leaderHellas Cena
Research projectGLUTTON

Tackling milk formula composition to improve infant nutrition


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Principal investigators

Antonio Dario Troise,Laura Cavallarin

Referred to

Spoke 06