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

C.L. Steffensen (Corresponding Author), Maija-Liisa Mattinen, Henrik Jørgen Andersen, Kristiina Kruus, Johanna Buchert, Jacob Holm Nielsen

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18 Citations (Scopus)

Abstract

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
Volume227
Issue number1
DOIs
Publication statusPublished - 2008
MoE publication typeA1 Journal article-refereed

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Keywords

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

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