In depth analysis of the contribution of specific glycoproteins to the overall bovine whey N-linked glycoprofile

Rivca L Valk-Weeber, Cecile Deelman-Driessen, Lubbert Dijkhuizen, Talitha Eshuis-de Ruiter, Sander van Leeuwen*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

2 Citations (Scopus)
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Abstract

The N-linked glycoprofile of bovine whey is the combined result of individual protein glycoprofiles. In this work, we provide in-depth structural information on the glycan structures of known whey glycoproteins, namely lactoferrin, lactoperoxidase, α-lactalbumin, immunoglobulin-G (IgG) and glycosylation dependent cellular adhesion molecule 1 (GlyCAM-1, PP3). The majority (~95%) of N-glycans present in the overall whey glycoprofile were attributed to three proteins; Lactoferrin, IgG and GlyCAM-1. We identified specific signature glycans for these main proteins; Lactoferrin contributes oligomannose-type glycans, while IgG carries fucosylated di-antennary glycans with Gal-β(1,4)GlcNAc (LacNAc) motifs. GlyCAM-1 is the sole whey glycoprotein carrying tri- and tetra-antennary structures, with a high degree of fucosylation and sialylation. Signature glycans can be used to recognize individual proteins in the overall whey glycoprofile, as well as for protein concentration estimations. Application of the whey glycoprofile analysis to colostrum samples revealed dynamic protein concentration changes for IgG, lactoferrin and GlyCAM-1 over time.

Original languageEnglish
Article numberacs.jafc.0c00959
Pages (from-to)6544-6553
Number of pages10
JournalJournal of Agricultural and Food Chemistry
Volume68
Issue number24
Early online date2020
DOIs
Publication statusPublished - 17-Jun-2020

Keywords

  • GlyCAM-1
  • PP3
  • colostrum
  • milk
  • protein glycosylation
  • whey

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