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

Research output: Contribution to journalArticleScientificpeer-review

17 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

Fingerprint

Coprinopsis cinerea
Coprinus
crosslinking
Hydrogen peroxide
Hydrogen Peroxide
Peptides
Peroxidase
hydrogen peroxide
Tyrosine
tyrosine
peroxidase
Polymerization
polymerization
peptides
Amino acids
Electron spin resonance spectroscopy
Proteins
Protein Engineering
Amino Acids
Biopolymers

Keywords

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

Cite this

Steffensen, C.L. ; Mattinen, Maija-Liisa ; Andersen, Henrik Jørgen ; Kruus, Kristiina ; Buchert, Johanna ; Holm Nielsen, Jacob. / Cross-linking of tyrosine-containing peptides by hydrogen peroxide-activated Coprinus Cinereus peroxidase. In: European Food Research and Technology. 2008 ; Vol. 227, No. 1. pp. 57 - 67.
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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.",
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Cross-linking of tyrosine-containing peptides by hydrogen peroxide-activated Coprinus Cinereus peroxidase. / Steffensen, C.L. (Corresponding Author); Mattinen, Maija-Liisa; Andersen, Henrik Jørgen; Kruus, Kristiina; Buchert, Johanna; Holm Nielsen, Jacob.

In: European Food Research and Technology, Vol. 227, No. 1, 2008, p. 57 - 67.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Cross-linking of tyrosine-containing peptides by hydrogen peroxide-activated Coprinus Cinereus peroxidase

AU - Steffensen, C.L.

AU - Mattinen, Maija-Liisa

AU - Andersen, Henrik Jørgen

AU - Kruus, Kristiina

AU - Buchert, Johanna

AU - Holm Nielsen, Jacob

PY - 2008

Y1 - 2008

N2 - 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.

AB - 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.

KW - Coprinus Cinereus peroxidase

KW - Cross-linking

KW - ESR

KW - MALDI-tof MS

KW - FTIR

KW - Tyrosyl radical

U2 - 10.1007/s00217-007-0692-y

DO - 10.1007/s00217-007-0692-y

M3 - Article

VL - 227

SP - 57

EP - 67

JO - European Food Research and Technology

JF - European Food Research and Technology

SN - 1438-2377

IS - 1

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