Journal of Protein Chemistry

, Volume 3, Issue 1, pp 35–48

Peroxidase-catalyzed cross linking of proteins

  • Gunter Matheis
  • John R. Whitaker

DOI: 10.1007/BF01024835

Cite this article as:
Matheis, G. & Whitaker, J.R. J Protein Chem (1984) 3: 35. doi:10.1007/BF01024835


Incubation of casein and water-soluble soybean protein, separately or together, at 10 mg/ml with horseradish peroxidase (2.4 or 24 μM) and H2O2 (1.8 or 18 mM) at pH 9.0 (0.2 M borate buffer) for 24 hr at 37°C in air led to formation of higher molecular weight compounds as determined by sodium dodecyl sulfate polyacrylamide disc gel electrophoresis. Incubation under the same conditions with peroxidase alone (in air) gave a smaller amount of higher molecular weight compounds. Incubation of lysozyme separately or with water-soluble soybean protein did not produce detectable amounts of higher molecular weight compounds. These results are discussed in terms of previously observed di- and tertyrosine isolated from peroxidase/H2O2-treated and naturally occurring proteins following acid hydrolysis. Transglutaminase, lipoxygenase, polyphenol oxidase, and lysyl oxidase are examples of other enzymes that can cross link proteins.

Key words

casein lysozyme water-soluble soybean protein peroxidase cross-linked proteins 

Copyright information

© Plenum Publishing Corporation 1984

Authors and Affiliations

  • Gunter Matheis
    • 1
  • John R. Whitaker
    • 1
  1. 1.Department of Food Science and TechnologyUniversity of CaliforniaDavis
  2. 2.SpringlbachWest Germany

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