## 1 Introduction  
Glycoproteins are a biologically important class of components with modulatory roles in signaling and cell adhesion. \(N\)-linked glycans are covalently bound to an asparagine residue with the consensus sequence on the primary structure of asparagine-X-serine/threonine (with X representing any amino acid besides proline) [1]. The attachment is mediated by the reducing end \(N\)-acetylglucosamine moiety of the glycan onto the asparagine residue [2]. All \(N\)-glycans share a common trimannosyl, chitobiose (two \(\beta\)-1,4 linked \(N\)-acetylglucosamine residues) core and are classified based on how the core is elongated with various monosaccharides. \(N\)-glycans can be decorated with \(N\)-acetylneuraminic acid or \(N\)-glycolheuraminic acid (sialylated) and/or fucose (fucosylated) in various antenary combinations to give rise to a heterogeneity of combinations, even on a single glycosylation site. Glycans can be classified based on their antennary decorations, with neutral, fucosylated, sialylated, and both fucosylated and sialylated being the primary non-plant glycans. As a model for understanding the interplay of indigestible carbohydrates and beneficial gut bacteria, human milk oligosaccharides (HMOs) have been widely studied and found to exhibit uniquely effective prebiotic functionalities [3]. While HMOs are quite abundant in human milk (up to 15 g/L in colostrum), their commercial-scale isolation from human milk is not feasible [4]. The activities and roles of intact and released \(N\)-linked glycans upon human consumption are not well understood due, in part, to the lack of adequate deglycosylation and analytic methods to release, identify, and quantity the released glycans [5]. \(N\)-glycans can be released from the protein moiety using harsh chemical treatments or enzymatic methods, the latter allowing for the recovery of intact protein and glycans. Deglycosylating enzymes include peptide-\(N\)-glycosases and endo-\(\beta\)-\(N\)-acetylglucosamine, which differ in cleavage points of the core of \(N\)-glycans [6]. Due to striking similarities in structures and functions, released \(N\)-linked glycans from bovine milk glycoproteins have been studied for their ability to promote the growth of commensal bacteria in vitro [7; 8]. A recently discovered endo-\(\beta\)-\(N\)-acetylglucosamineamidase (Endo-BI-1), isolated from _B. infantits_, was shown to deglycosylate human milk glycoproteins more effectively than other endo-\(\beta\)-\(N\)-acetylglucosamineamidase isolated from several commensal _Bifidobacterium_ species [9]. More importantly, released \(N\)-glycans by this novel enzyme from bovine milk proteins displayed a remarkable selective prebiotic activity on _Bifidobacterium longum_ subsp. _infantits_ in vitro, and may promote the growth of other beneficial bacteria while inhibiting pathogens [7; 8; 10]. However, to establish \(N\)-glycans as an alternative source of prebiotic carbohydrates to human milk, further research into the selectivity of bovine \(N\)-glycans and their functional similarity with HMOs with respect to commensal, beneficial, and pathogenic gut organisms is necessary. Whey, the co-product of cheese manufacture, is a potential commercially available source of underutilized glycoproteins. The concentration of proteins in bovine cheese whey ranges from 1 to 2%, wherein approximately 4-9% of those proteins are \(N\)-glycosated immunoglobulins, lactoferrin, and transferrin [11; 12]. Lactoferrin, while found in substantial quantities in human milk and bovine colostrum, is present in bovine milk and cheese whey at the trace level. Yet, the nearly 200 million tonnes of whey produced each year globally [13] conservatively translates to 2 million tonnes of whey proteins, corresponding to approximately 100,000 tonnes of bovine milk glycoproteins available for subsequent processing.