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The primary proteins in chicken egg white are glycoproteins, which generate substantial glycopeptides in the digestive tract following gastrointestinal digestion. The structures of the glycopeptides have yet to be identified and elucidated. In this study, chicken egg white was digested by trypsin, and N-glycopeptides were enriched from the hydrolysate by hydrophilic interaction chromatography and O-glycopeptides by retain AX chromatography combined with AminoLink resin adsorption. The structures of these glycopeptides were analyzed by liquid chromatography-mass spectrometry (LC-MS), and their potential intestinal effects were explored by bioinformatics analysis. Mass spectrometry analysis identified 1 720 N-glycopeptides from 49 N-glycoproteins and 565 O-glycopeptides from 29 O-glycoproteins. Glycopeptides derived from ovomucin were the most diverse, including 490 N-glycopeptides and 216 O-glycopeptides. Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway enrichment analysis revealed that sialylated N-glycoproteins were mainly involved in interleukin-17 signaling pathway and ferroptosis, while sialylated O-glycoproteins were mainly involved in cholesterol metabolism, vitamin digestion and absorption, the hypoxia-inducible factor-1 signaling pathway and the renin-angiotensin system. This study provides crucial structural information for further research on the potential effects of egg white glycopeptides on the intestinal tract.

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Copyright of Food Research & Development is the property of Food Research & Development Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

The cardiovascular system, a complicated and delicate closed circulatory system, is regulated by various protein post-translational modifications, in which N-glycosylation plays a crucial role. N-glycosylation of nascent peptide chains is a co-translation or post-translational modification. Inrecent years, increasing investigations have demonstrated that N-glycosylation is implicated in the regulation of cardiovascular function by affecting the location and function of numerous essential proteins, further participates in the incidence and progression of various cardiovascular-related diseases, including hypertension, arrhythmia, atherosclerosis, etc. This review focuses on the role of protein N-glycosylation and its potential therapeutic implications in diverse cardiovascular diseases. [ABSTRACT FROM AUTHOR]

Copyright of Journal of Agricultural Science & Technology (1008-0864) is the property of Journal of Agricultural Science & Technology and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

IFN-λ1 is a member of a new family of interferons called type Ⅲ IFNs with similar functions to type ⅠIFNs. Previously we obtained recombinant soluble human rhIFN-λ1 from Pichia pastoris. However, the hyper-glycosylation from P. pastoris brings immunogenicity and low purification recovery rate. To overcome this disadvantage, in this study, we constructed an rhIFN-λ1 mutant (rhIFN-λ1-Nm) devoid of the potential N-glycosylation sites by site-directed mutagenesis. rhIFN-λ1-Nm was successfully expressed and secreted extracellularly in P. pastoris (GS115) using methanol inducible AOX1 promoter with α-mating factor signal sequence. rhIFN-λ1-Nm was purified and characterized. There was no significant difference between rhIFN-λ1-Nm and rhIFN-λ1 in structure and bioactivity. The molecular weight was low after N-glycosylation mutation whereas the glycosylation was much lower. The mutational rhIFN-λ1 (rhIFN-λ1-Nm) could legitimately be developed as substitutes for rhIFN-λ1, and thus it may be developed into a more promising therapeutic reagent in the future.