Skip to main content
SpringerLink
Log in

Studies on the impact of glycation on the denaturation of whey proteins

  • Original Paper
  • Published:
European Food Research and Technology Aims and scope Submit manuscript

Abstract

It could be shown for technologically relevant whey protein powders that denaturation of β-lactoglobulin (β-Lg) is affected significantly by the extent of covalent modification of lysine residues by lactose. The amount of acid soluble β-Lg as measured via RP-HPLC with UV detection after heating for 10 min at 80 °C increased from 40% (4.6% lysine modification) to 82% (22.4% lysine modification). An increase in glycation leads to a slower denaturation-induced oligomerisation, as shown by SDS-PAGE. Concomitant with an increase in lysine modification, the denaturation temperature increased from 79.5 to 84 °C, as measured by differential scanning calorimetry (DSC). Covalent attachment of lactose to whey proteins during preparation or storage significantly improves the heat stability of whey proteins, which may be of particular importance for the technological use of whey proteins varying in the degree of lysine modification.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5
Fig. 6

Similar content being viewed by others

References

  1. Foegeding EA, Kuhn PR, Hardin CC (1992) J Agric Food Chem 40:2092–2097

    Article  CAS  Google Scholar 

  2. Lorenzen PC, Schrader KA (2006) Lait 86:259–271

    Article  CAS  Google Scholar 

  3. Damodaran S (1997) Protein-stabilized foams and emulsions. In: Damodaran S, Paraf A (eds) Food proteins and their applications. Marcel Dekker, New York, pp 57–110

    Google Scholar 

  4. Alvarez Gomez JM, Rodriguez PJ (2006) Ind Eng Chem Res 45:7510–7519

    Article  CAS  Google Scholar 

  5. Pearce KN, Kinsella JE (1978) J Agric Food Chem 26:716–723

    Article  CAS  Google Scholar 

  6. Kinsella JE, Whitehead DM (1989) Adv Food Nutr Res 33:343–438

    Article  CAS  Google Scholar 

  7. Bertrand-Harb C, Baday A, Dalgalarrondo M, Chobert J-M, Haertle T (2002) Nahrung 46:283–289

    Article  CAS  Google Scholar 

  8. Leonil J, Molle D, Fauquant J, Maubois JL, Pearce RJ, Bouhallab S (1997) J Dairy Sci 80:2270–2281

    Article  CAS  Google Scholar 

  9. Morgan F, Leonil J, Molle D, Bouhallab S (1997) Biochem Biophys Res Commun 236:413–417

    Article  CAS  Google Scholar 

  10. Henle T (2005) Amino Acids 29:313–322

    Article  CAS  Google Scholar 

  11. Chobert J-M, Gaudin J-C, Dalgalarrondo M, Haertlé T (2006) Biotechnol Adv 24:629–632

    Article  CAS  Google Scholar 

  12. Bouhallab S, Morgan F, Gwenaeele H, Molle D, Leonil J (1999) J Agric Food Chem 47:1489–1494

    Article  CAS  Google Scholar 

  13. Van Teeffelen AMM, Broersen K, De Jongh HHJ (2005) Protein Sci 14:2187–2194

    Article  CAS  Google Scholar 

  14. Broersen K, Vorhagen AGJ, Hamer RJ, De Jongh HHJ (2004) Milchwiss 51:509–512

    Google Scholar 

  15. Henle T, Walter AW, Klostermeyer H (1993) Z Lebensm Unters Forsch 197:114–117

    Article  CAS  Google Scholar 

  16. Krause R, Knoll K, Henle T (2003) Eur Food Res Technol 216:277–283

    CAS  Google Scholar 

  17. Jenness R, Koops J (1962) Neth Milk Dairy J 16:153–164

    CAS  Google Scholar 

  18. IDF-Standard 178:2005

  19. Westermeier R (1997) Electrophoresis in practice, 2nd edn, VCH, Weinheim

  20. Erbersdobler HF, Somoza V (2007) Mol Nutr Food Res 51:423–430

    Article  CAS  Google Scholar 

  21. Finot PA, Deutsch R, Bujard E (1981) Prog Food Nutr Sci 5:344–355

    Google Scholar 

  22. Morales F-J, Romero C, Jiménez-Pérez S (2000) Int J Food Sci Technol 35:193–200

    Article  CAS  Google Scholar 

  23. Spiegel T (1999) Int J Food Sci Technol 34:523–531

    Article  CAS  Google Scholar 

  24. Relkin P (1994) Thermochim Acta 246:371–386

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Institute of Food Chemistry, Technische Universität Dresden, 01062, Dresden, Germany

    Bozena B. Mulsow, Mandy Jacob & Thomas Henle

Authors
  1. Bozena B. Mulsow
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Mandy Jacob
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Thomas Henle
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Thomas Henle.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Mulsow, B.B., Jacob, M. & Henle, T. Studies on the impact of glycation on the denaturation of whey proteins. Eur Food Res Technol 228, 643–649 (2009). https://doi.org/10.1007/s00217-008-0973-0

Download citation

  • Received:

  • Revised:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s00217-008-0973-0

Keywords

Search

Navigation