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    Application of industrial treatments to donor human milk: influence of pasteurization treatments, storage temperature, and time on human milk gangliosides
    (Springernature, 2018) Salcedo, Jaime; Karav, Sercan; Le Parc, Annabelle; Cohen, Joshua L.; de Moura Bell, Juliana M. L. N.; Sun, Adam; Lange, Matthew C.
    Donor milk is the best option when mother's own milk is unavailable. Heat treatments are applied to ensure donor milk safety. The effects of heat treatments on milk gangliosides-bioactive compounds with beneficial antibacterial, anti-inflammatory, and prebiotic roles-have not been studied. The most abundant gangliosides in non-homogenized human milk were characterized and quantified by liquid chromatography-mass spectrometry (LC-MS)/MS before and after pasteurization treatments mimicking industrial conditions (63 degrees C/30 min, 72 degrees C/15 s, 127 degrees C/5 s, and 140 degrees C/6 s). Ganglioside stability over a 3-month period was assessed following the storage at 4 and 23 degrees C. Independent of the heat treatment applied, gangliosides were stable after 3 months of storage at 4 or 23 degrees C, with only minor variations in individual ganglioside structures. These findings will help to define the ideal processing and storage conditions for donor milk to maximize the preservation of the structure of bioactive compounds to enhance the health of fragile newborns. Moreover, these results highlight the need for, and provide a basis for, a standardized language enabling biological and food companies, regulatory agencies, and other food stakeholders to both annotate and compute the ways in which production, processing, and storage conditions alter or maintain the nutritive, bioactive, and organoleptic properties of ingredients and foods, as well as the qualitative effects these foods and ingredients may have on conferring phenotype in the consuming organism. Donor milk treatment: key nutrients preserved after pasteurization Donor human milk, the best alternative to mother's own milk, usually needs to be pasteurized before use out of safety concerns. Daniela Barile at University of California Davis, USA, and colleagues studied the effects of heat treatment and storage temperature and time on milk gangliosides, a class of sugar-derived compounds important for neural and brain development of newborns, among other bioactivities. They found that, while there were minor structural changes during mimicked industrial pasteurization processes, gangliosides remain stable for at least three months either in the refrigerator or at room temperature. These results may help standardize the processing protocols and storage conditions for donor milk, and the methods can be extended to other bioactive components.
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    Characterization of recombinant human lactoferrin N-glycans expressed in the milk of transgenic cows
    (Public Library Science, 2017) Le Parc, Annabelle; Karav, Sercan; Rouquie, Camille; Maga, Elizabeth A.; Bunyatratchata, Apichaya; Barile, Daniela
    Lactoferrin (LF) is one of the most abundant bioactive glycoproteins in human milk. Glycans attached through N-glycosidic bonds may contribute to Lactoferrin functional activities. In contrast, LF is present in trace amounts in bovine milk. Efforts to increase LF concentration in bovine milk led to alternative approaches using transgenic cows to express human lactoferrin (hLF). This study investigated and compared N-glycans in recombinant human lactoferrin (rhLF), bovine lactoferrin (bLF) and human lactoferrin by Nano-LC-Chip-Q-TOF Mass Spectrometry. The results revealed a high diversity of N-glycan structures, including fucosylated and sialylated complex glycans that may contribute additional bioactivities. rhLF, bLF and hLF had 23, 27 and 18 N-glycans respectively with 8 N-glycan in common overall. rhLF shared 16 N-glycan with bLF and 9 N-glycan with hLF while bLF shared 10 N-glycan with hLF. Based on the relative abundances of N-glycan types, rhLF and hLF appeared to contain mostly neutral complex/ hybrid N-glycans (81% and 52% of the total respectively) whereas bLF was characterized by high mannose glycans (65%). Interestingly, the majority of hLF N-glycans were fucosylated (88%), whereas bLF and rhLF had only 9% and 20% fucosylation, respectively. Overall, this study suggests that rhLF N-glycans share more similarities to bLF than hLF.
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    Studying Lactoferrin N-Glycosylation
    (Mdpi, 2017) Karav, Sercan; German, J. Bruce; Rouquie, Camille; Le Parc, Annabelle; Barile, Daniela
    Lactoferrin is a multifunctional glycoprotein found in the milk of most mammals. In addition to its well-known role of binding iron, lactoferrin carries many important biological functions, including the promotion of cell proliferation and differentiation, and as an anti-bacterial, anti-viral, and anti-parasitic protein. These functions differ among lactoferrin homologs in mammals. Although considerable attention has been given to the many functions of lactoferrin, its primary nutritional contribution is presumed to be related to its iron-binding characteristics, whereas the role of glycosylation has been neglected. Given the critical role of glycan binding in many biological processes, the glycan moieties in lactoferrin are likely to contribute significantly to the biological roles of lactoferrin. Despite the high amino acid sequence homology in different lactoferrins (up to 99%), each exhibits a unique glycosylation pattern that may be responsible for heterogeneity of the biological properties of lactoferrins. An important task for the production of biotherapeutics and medical foods containing bioactive glycoproteins is the assessment of the contributions of individual glycans to the observed bioactivities. This review examines how the study of lactoferrin glycosylation patterns can increase our understanding of lactoferrin functionality.