Enzymatic modification of wool with tyrosinase and peroxidase

Raija Lantto (Corresponding Author), E. Heine, G. Freddi, Arja Lappalainen, Arja Miettinen-Oinonen, Marja-Leena Niku-Paavola, Johanna Buchert

Research output: Contribution to journalArticleScientificpeer-review

23 Citations (Scopus)


The capabilities of tyrosinase and peroxidase to activate tyrosine residues of wool fibres and to catalyze crosslink formation between peptides derived from a wool protein hydrolyzate were investigated. Peroxidases were able to catalyse oxidation of wool fibres corresponding to 35–40% of the tyrosine residues located on the wool surface or 2% of the tyrosine residues in the wool fibre. Similar fibre surface modification was detected with tyrosinase and a fungal peroxidase using x-ray photoelectron spectroscopy. Tyrosinase did not show detectable activation of fibres measured as oxygen consumption. Tyrosinase was, however, able to crosslink peptides of 3–10 kDa derived from enzymatically hydrolysed wool fibres. Surprisingly, no crosslinking was detected with peroxidase.
Original languageEnglish
Pages (from-to)109 - 116
Number of pages8
JournalJournal of the Textile Institute
Issue number2
Publication statusPublished - 2005
MoE publication typeA1 Journal article-refereed


  • proteinaceous fibre
  • enzyme treatment
  • cross-linking
  • tyrosine
  • peroxidase
  • tyrosinase

Fingerprint Dive into the research topics of 'Enzymatic modification of wool with tyrosinase and peroxidase'. Together they form a unique fingerprint.

Cite this