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Amino Acids

pp 1–11 | Cite as

Diversity of advanced glycation end products in the bovine milk proteome

  • Sanja Milkovska-StamenovaEmail author
  • Ralf HoffmannEmail author
Original Article
  • 29 Downloads

Abstract

Milk processing relies on thermal treatments warranting microbiologically safe products with extended shelf life. However, elevated temperatures favor also Maillard reactions yielding the structurally diverse advanced glycation end products (AGEs). AGEs may alter protein functions and immunogenicity and also decrease the nutritional value of milk products. Furthermore, dietary AGEs contribute to the circulating AGE pool with potentially harmful effects. Here, 14 types of protein-derived AGEs present in raw milk or produced during processing/storage of regular and lactose-free milk products were identified by nanoRP-UPLC-ESI–MS/MS. In total, 132 peptides (118 modification sites in 62 proteins) were modified by at least one studied AGE. Amide-AGEs were the most abundant group with formyllysine being the main type. Most lysine- and arginine-derived AGEs and their modification sites have not been reported before. The number of AGE modification sites increased with the harsher processing conditions of regular milk, but remained stable during storage. This was further supported by quantitative data.

Keywords

Advanced glycation end products Amide-AGEs Dairy products Milk processing Shelf life storage 

Notes

Acknowledgements

We kindly thank Michele Wölk for performing an experiment to exclude formyllysine formation during the sample preparation procedure. Financial support from the Deutsche Forschungsgemeinschaft (HO2222/7-1, INST 268/289-1) and the European Fund for Regional Structure Development (EFRE, European Union and Free State Saxony; 100055720, 100092961 and 100146238) is gratefully acknowledged.

Compliance with ethical standards

Conflicts of interest

None.

Supplementary material

726_2019_2707_MOESM1_ESM.docx (9.5 mb)
Supplementary material 1 (DOCX 9755 kb) Table S1 AGE-modified peptides and the corresponding modification sites. Table S2 AGE-modified milk proteins and their modification sites. Fig. S1 SDS-PAGE of milk proteins precipitated from commercial milk products. Fig. S2 SDS-PAGE of tryptic digests of milk proteins. Fig. S3 Strategy applied for the identification of AGEs in bovine milk proteins. Fig. S4 Structures of Lys- and Arg-derived AGEs. Fig. S5 CID and ETD tandem mass spectra of a CML-modified tryptic peptide. Fig. S6 CID and ETD tandem mass spectra of a pyralline-, FL and CML-modified tryptic peptides. Fig. S7 TICs and XICs of peptide 77 for a UHT-treated sample processed with formic acid or TFA. Fig. S8 Peak areas of peptides 7, 66, and 78 determined in a UHT-treated sample processed with formic acid or TFA. Fig. S9 Number of AGE-modified peptides derived from β-lactoglobulin. Fig. S10 Relative quantification of AGE-modified peptides of β-lactoglobulin

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Copyright information

© Springer-Verlag GmbH Austria, part of Springer Nature 2019

Authors and Affiliations

  1. 1.Institute of Bioanalytical Chemistry, Faculty of Chemistry and MineralogyUniversität LeipzigLeipzigGermany
  2. 2.Center for Biotechnology and BiomedicineUniversität LeipzigLeipzigGermany

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