Heat Induced Crosslinks in Milk Proteins and Consequences for the Milk System

  • Henning Klostermeyer
  • Ernst H. Reimerdes
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 86)


The protein system of milk is rather unusual, there are nearly no interchain crosslinks found. Even intrachain crosslinks, especially disulfide bridges, are present only in about every fourth protein molecule. Heating causes dramatic changes in the structure of milk proteins, resulting in the formation of polymeric networks. The contribution of individual milk proteins, namely the ß-lactoglobulins, α-lactalbumin and æ-casein, to the formation of crosslinks is studied with respect to heating temperature and time, pH and atmosphere. Measured are changes in molecular weights and in the SH/SS-levels as well as the formation of dehydroalanine, lysinoalanine, lanthionine and isopeptide bonds. Some practical aspects of crosslinking in milk proteins are discussed.


Proline Lysin Disulfide Thiol Lactose 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Springer Science+Business Media New York 1977

Authors and Affiliations

  • Henning Klostermeyer
    • 1
  • Ernst H. Reimerdes
    • 1
  1. 1.Institut für ChemieBundesanstalt für MilchforschungKielGermany

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