TitleCharacterization of goat milk lactoferrin N-glycans and comparison with the N-glycomes of human and bovine milk.
Publication TypeJournal Article
Year of Publication2014
AuthorsLe Parc, A, Dallas, DC, Duaut, S, Leonil, J, Martin, P, Barile, D
JournalElectrophoresis
Volume35
Issue11
Pagination1560-70
Date Published2014 Jun
ISSN1522-2683
KeywordsAmino Acid Sequence, Animals, Carbohydrate Sequence, Cattle, Chromatography, High Pressure Liquid, Glycomics, Goats, Humans, Lactoferrin, Milk, Molecular Sequence Data, Polysaccharides, Tandem Mass Spectrometry
Abstract
 

Numerous milk components, such as lactoferrin, are recognized as health-promoting compounds. A growing body of evidence suggests that glycans could mediate lactoferrin's bioactivity. Goat milk lactoferrin is a candidate for infant formula supplementation because of its high homology with its human counterpart. The aim of this study was to characterize the glycosylation pattern of goat milk lactoferrin. After the protein was isolated from milk by affinity chromatography, N-glycans were enzymatically released and a complete characterization of glycan composition was carried out by advanced MS. The glycosylation of goat milk lactoferrin was compared with that of human and bovine milk glycoproteins. Nano-LC-Chip-Q-TOF MS data identified 65 structures, including high mannose, hybrid, and complex N-glycans. Among the N-glycan compositions, 37% were sialylated and 34% were fucosylated. The results demonstrated the existence of similar glycans in human and goat milk but also identified novel glycans in goat milk that were not present in human milk. These data suggest that goat milk could be a source of bioactive compounds, including lactoferrin that could be used as functional ingredients for food products beneficial to human nutrition.

DOI10.1002/elps.201300619
Alternate JournalElectrophoresis
PubMed ID24519758
PubMed Central IDPMC4048649
Grant ListR01 AT007079 / AT / NCCIH NIH HHS / United States
R01AT007079 / AT / NCCIH NIH HHS / United States