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dc.contributor.authorMarino, Karina
dc.contributor.authorLane, Jonathan A.
dc.contributor.authorAbrahams, Jodie L.
dc.contributor.authorStruwe, Weston B.
dc.contributor.authorHarvey, David J.
dc.contributor.authorMarotta, Mariarosaria
dc.contributor.authorHickey, Rita M.
dc.contributor.authorRudd, Pauline M.
dc.date.accessioned2017-08-11T03:17:35Z
dc.date.available2017-08-11T03:17:35Z
dc.date.issued2011
dc.identifier.issn0959-6658
dc.identifier.doi10.1093/glycob/cwr067
dc.identifier.urihttp://hdl.handle.net/10072/343818
dc.description.abstractAlthough the properties of milk oligosaccharides have been of scientific interest for many years, their structural diversity presents a challenging analytical task. In the quest for a simple and robust technology to characterize the different oligosaccharides present in milk, we developed an analytical scheme based on their fluorescent labeling, pre-fractionation by weak anionic exchange chromatography and separation by hydrophilic interaction liquid chromatography (HILIC)-high performance liquid chromatography (HPLC). HILIC relies on the hydrophilic potential of the molecule, which accounts for differences in properties such as molecular volume, lipophilic surface area, charge, composition, structure, linkage and oligosaccharide branching. The robustness of the methodology has been demonstrated using bovine colostrum oligosaccharides as a case study. Structural assignments for 37 free glycans, including 20 sialylated species, were obtained by a combination of HILIC-HPLC, exoglycosidase digestion and offline negative-ion mode mass spectrometry (MS)/MS. Parameters obtained for each glycan, including linkages, enzymatic digestion products and glucose unit values, will be added to GlycoBase, a public access database (http://glycobase.nibrt.ie/glycobase.html). This approach provides a basis for the analysis of free milk oligosaccharides in a fast and sensitive manner and could be adapted for an automated technology platform amenable to diverse environments. Indeed, our approach, in conjunction with bacterial-binding assays, can provide a better understanding of the structural elements required for biological activity of free milk oligosaccharides and could serve as a scientific basis for the selection of such bioactives from various food sources.
dc.description.peerreviewedYes
dc.languageEnglish
dc.language.isoeng
dc.publisherOxford University Press
dc.relation.ispartofpagefrom1317
dc.relation.ispartofpageto1330
dc.relation.ispartofissue10
dc.relation.ispartofjournalGlycobiology
dc.relation.ispartofvolume21
dc.subject.fieldofresearchBiochemistry and Cell Biology not elsewhere classified
dc.subject.fieldofresearchBiological Sciences
dc.subject.fieldofresearchMedical and Health Sciences
dc.subject.fieldofresearchcode060199
dc.subject.fieldofresearchcode06
dc.subject.fieldofresearchcode11
dc.titleMethod for milk oligosaccharide profiling by 2-aminobenzamide labeling and hydrophilic interaction chromatography
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.hasfulltextNo Full Text
gro.griffith.authorAbrahams, Jodie L.


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