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Article 2023 · 3 atıf

Utilizing linkage-specific ethyl-esterification approach to perform in-depth analysis of sialylated N-glycans present on milk whey glycoproteins

Kayili, Haci Mehmet, Barlas, Nazire, Demirhan, Deniz Baran, Yaman, Mehmet Emrah, Atakay, Mehmet, Guler, Ulku, Kara, Mustafa, Tekgunduz, Kadir Serafettin, Salih, Bekir

Özet

Glycosylation 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.

Anahtar Kelimeler
Milk Glycomics Ethyl-esterification Whey glycoproteins MALDI-MS N-glycans BOVINE OLIGOSACCHARIDES GLYCOSYLATION PROTEINS GLYCOME
WoS Kategorileri
Chemistry, Applied Food Science & Technology Nutrition & Dietetics
Sürdürülebilir Kalkınma Amaçları
Künye
Dergi
FOOD CHEMISTRY
Yıl
2023
Cilt
421
ISSN
0308-8146
eISSN
1873-7072
DOI
10.1016/j.foodchem.2023.136166
WoS UID
WOS:000983681600001
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