Cross-linking of tyrosine-containing peptides by hydrogen peroxide-activated Coprinus Cinereus peroxidase

Charlotte Langgaard Steffensen, Maija Liisa Mattinen, Henrik Jørgen Andersen, Kristiina Kruus, Johanna Buchert, Jacob Holm Nielsen

Research output: Contribution to journalArticleScientificpeer-review

21 Citations (Scopus)


Hydrogen peroxide-activated Coprinus Cinereus peroxidase (CIP) can initiate polymerization of tyrosine-containing peptides via initial formation of an intermediate tyrosyl radical, which for the first time has been identified by spin trap electron spin resonance spectroscopy as located on carbon 1 in the aromatic ring, and subsequent formation of either dityrosine or isodityrosine bonds through a net elimination of two hydrogen atoms between peptides. The rate and degree of polymerization were found to depend on peptide size and the amino acid adjacent to tyrosine, as longer peptides and amino acids with bulky side groups were less reactive. In the forwarded hypothesis for the reaction mechanism upon peroxidase-initiated cross-linking of tyrosine-containing peptides and proteins, it is suggested that the polymerization takes place through a radical chain reaction. The polymerization reaction shows the potential of CIP as a protein structure-engineering tool to control functionality of proteinious food matrices or in biopolymer formation.

Original languageEnglish
Pages (from-to)57-67
Number of pages11
JournalEuropean Food Research and Technology
Issue number1
Publication statusPublished - 1 May 2008
MoE publication typeA1 Journal article-refereed


  • Coprinus Cinereus peroxidase
  • Cross-linking
  • ESR
  • FTIR
  • MALDI-tof MS
  • Tyrosyl radical


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