Kayili, Haci MehmetBarlas, NazireDemirhan, Deniz BaranYaman, Mehmet EmrahAtakay, MehmetGuler, UlkuKara, Mustafa2024-09-292024-09-2920230308-81461873-7072https://doi.org/10.1016/j.foodchem.2023.136166https://hdl.handle.net/20.500.14619/4652Glycosylation of milk whey proteins, specifically the presence of sialic acid-containing glycan residues, causes functional changes in these proteins. This study aimed to analyze the N-glycome of milk whey glycoproteins from various milk sources using a linkage-specific ethyl esterification approach with MALDI-MS (matrix-assisted laser desorption/ionization-mass spectrometry). The results showed that the N-glycan profiles of bovine and buffalo whey mostly overlapped. Acetylated N-glycans were only detected in donkey milk whey at a rate of 16.06%. a2,6-linked N-Acetylneuraminic acid (a2,6-linked NeuAc, E) was found to be the predominant sialylation type in human milk whey (65.16%). The amount of a2,6-linked NeuAc in bovine, buffalo, goat, and donkey whey glycoproteomes was 42.33%, 44.16%, 39.00%, and 34.86%, respectively. The relative abundances of a2,6-linked N-Glycolylneuraminic acid (a2,6-linked NeuGc, Ge) in bovine, buffalo, goat, and donkey whey were 7.52%, 5.41%, 28.24%, and 17.31%, respectively. Goat whey exhibited the highest amount of a2,3-linked N-Glycolylneuraminic acid (a2,3-linked NeuGc, Gl, 8.62%), while bovine and donkey whey contained only 2.14% and 1.11%, respectively.eninfo:eu-repo/semantics/closedAccessMilkGlycomicsEthyl-esterificationWhey glycoproteinsMALDI-MSN-glycansArticle10.1016/j.foodchem.2023.1361662-s2.0-8515349629937086518Q1421WOS:000983681600001Q1