Glycoproteomics reveal differences in site-specific N-glycosylation of whey proteins between donkey colostrum and mature milk

Guan, Boyuan; Gao, Yang; Chai, Yuxia; Amantai, Xiakouna; Chen, Xinping; Cao, Xiaohong; Yue, Xiqing

doi:10.1016/j.lwt.2022.113920

Cited by 3 publications

(3 citation statements)

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“…In addition, the use of proteomics to demonstrate changes in donkey milk protein and glycoprotein levels during lactation has also been reported. Guan et al identified donkey MFGM, whey N-glycoproteins, and site-specific N-glycosylation during lactation using label-free site-specific glycoproteomics. , 409 intact N-glycopeptides from 86 glycoproteins in DM and 1443 intact N-glycopeptides from 336 glycoproteins in DC were identified. For whey proteins, DC contained 685 intact N-glycopeptides from 135 glycoproteins, whereas DM contained 384 intact N-glycopeptides from 67 glycoproteins.…”

Section: Proteome-based Investigation Of the Effects Of Protein Analy...mentioning

confidence: 99%

Proteomics and Peptidomics As a Tool to Compare the Proteins and Endogenous Peptides in Human, Cow, and Donkey Milk

Ning,

Yang,

Liu

et al. 2023

J. Agric. Food Chem.

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Cow’s milk is the most widely used ingredient in infant formulas. However, its specific protein composition can cause allergic reactions. Finding alternatives to replace cow’s milk and fill the nutritional gap with human milk is essential for the health of infants. Proteomic and peptidomic techniques have supported the elucidation of milk’s nutritional ingredients. Recently, omics approaches have attracted increasing interest in the investigation of milk because of their high throughput, precision, sensitivity, and reproducibility. This review offers a significant overview of recent developments in proteomics and peptidomics used to study the differences in human, cow, and donkey milk. All three types of milks were identified to have critical biological functions in human health, particularly in infants. Donkey milk proteins were closer in composition to human milk, were less likely to cause allergic reactions, and may be developed as novel raw materials for formula milk powders.

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Section: Proteome-based Investigation Of the Effects Of Protein Analy...mentioning

confidence: 99%

Proteomics and Peptidomics As a Tool to Compare the Proteins and Endogenous Peptides in Human, Cow, and Donkey Milk

Ning,

Yang,

Liu

et al. 2023

J. Agric. Food Chem.

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“…The identification of proteins, metabolites, and free fatty acids in donkey colostrum has been carried out. [21][22][23][24][25][26] Guan et al conducted a comparison of glycoproteins, glycopeptides, and glycosylation sites in whey proteins in donkey colostrum and mature milk. During lactation, a total of 164 whey proteins from donkey milk were analysed, revealing the presence of 946 N-glycopeptides.…”

Section: Introductionmentioning

confidence: 99%

“…Among them, 42 N -glycopeptides originating from 42 whey proteins exhibited significant differences between the two groups. 21 Garhwal et al conducted a study to investigate the variation in metabolites present in donkey milk during different stages of lactation. A total of 36 metabolites were identified in Halari donkey colostrum and mature milk.…”

Section: Introductionmentioning

confidence: 99%

Characterization and biological function analysis of endogenous peptides derived from donkey colostrum proteins

Ning,

Li,

Chen

et al. 2023

Food Funct.

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New insights into site‐specific N‐glycosylation profiling differences of serum proteomes between colostrum and mature breast milk

et al. 2023

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N‐glycosylation has important implications for the physicochemical properties and biochemical activity of breast milk proteins. However, an in‐depth characterization of site‐specific N‐glycans in breast milk serum proteins is lacking. In this study, 875 site‐specific N‐glycans attached to 114 serum glycoproteins from breast colostrum (BC) and 427 site‐specific N‐glycans attached to 60 serum glycoproteins from breast mature milk (BM) were identified and quantified using label‐free site‐specific glycoproteomics. Among them, 24 site‐specific N‐glycans mapping to 11 N‐glycosites on 9 glycoproteins were significantly increased, and 76 site‐specific N‐glycans mapping to 19 N‐glycosites on 13 glycoproteins were significantly decreased. Gene ontology annotation analysis showed that BC and BM serum N‐glycoproteins were mainly enriched in complement activation, classical pathway, extracellular exosome part, and immunoglobulin receptor binding. Kyoto Encyclopedia of Genes and Genomes pathway analysis revealed that BC and BM serum N‐glycoproteins were mainly involved in the PI3K‐Akt signaling pathway. Additionally, breast milk serum N‐glycoproteins carried fucosylated core structures as well as Lewis and sialylated branch structures that may contribute to neonatal retinal homeostasis. These results provide a molecular basis for understanding the unique biological activities of breast milk serum N‐glycoproteins.

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Glycoproteomics reveal differences in site-specific N-glycosylation of whey proteins between donkey colostrum and mature milk

Cited by 3 publications

References 40 publications

Proteomics and Peptidomics As a Tool to Compare the Proteins and Endogenous Peptides in Human, Cow, and Donkey Milk

Proteomics and Peptidomics As a Tool to Compare the Proteins and Endogenous Peptides in Human, Cow, and Donkey Milk

Characterization and biological function analysis of endogenous peptides derived from donkey colostrum proteins

New insights into site‐specific N‐glycosylation profiling differences of serum proteomes between colostrum and mature breast milk

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