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

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23 Citations (Scopus)

Abstract

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
Volume96
Issue number2
DOIs
Publication statusPublished - 2005
MoE publication typeA1 Journal article-refereed

Keywords

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

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  • Cite this

    Lantto, R., Heine, E., Freddi, G., Lappalainen, A., Miettinen-Oinonen, A., Niku-Paavola, M-L., & Buchert, J. (2005). Enzymatic modification of wool with tyrosinase and peroxidase. Journal of the Textile Institute, 96(2), 109 - 116. https://doi.org/10.1533/joti.2004.0080