| Makale Türü | Özgün Makale (SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale) | ||
| Dergi Adı | Food Chemistry (Q1) | ||
| Dergi ISSN | 0308-8146 Dergi Bilgileri (2023) | ||
| Dergi Tarandığı Indeksler | SCI-Expanded | ||
| Makale Dili | Türkçe | Basım Tarihi | 09-2023 |
| Cilt / Sayı / Sayfa | 421 / 1 / 136166–0 | DOI | 10.1016/j.foodchem.2023.136166 |
| Makale Linki | http://dx.doi.org/10.1016/j.foodchem.2023.136166 | ||
| UAK Araştırma Alanları |
Analitik Kimya
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| 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 … |
| Anahtar Kelimeler |
| Ethyl-esterification | Glycomics | MALDI-MS | Milk | N-glycans | Whey glycoproteins |
| Atıf Sayıları | |
| Web of Science | 3 |
| Scopus | 4 |
| Google Scholar | 5 |
| Dergi Adı | Food Chemistry |
| Kısa Adı | FOOD CHEM |
| Yayıncı | ELSEVIER SCI LTD |
| Açık Erişim | Evet |
| ISSN | 0308-8146 |
| E-ISSN | 1873-7072 |
| Wos Quartile | Q1 |
| Scopus Quartile | Q1 |
| Tarandığı Indeksler | SCIE , Scopus |
| WoS Kategoriler | CHEMISTRY, APPLIED | FOOD SCIENCE & TECHNOLOGY | NUTRITION & DIETETICS |
| Scopus Kategoriler | ANALYTICAL CHEMISTRY | FOOD SCIENCE | MEDICINE (MISCELLANEOUS) |