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

22 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

Fingerprint

Wool fibers
Monophenol Monooxygenase
Wool
catechol oxidase
wool
Peroxidase
peroxidase
Peptides
Tyrosine
tyrosine
Peroxidases
Fibers
Photoelectron spectroscopy
peptides
Crosslinking
Surface treatment
Photoelectron Spectroscopy
peroxidases
Chemical activation
Oxygen

Keywords

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

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
Lantto, Raija ; Heine, E. ; Freddi, G. ; Lappalainen, Arja ; Miettinen-Oinonen, Arja ; Niku-Paavola, Marja-Leena ; Buchert, Johanna. / Enzymatic modification of wool with tyrosinase and peroxidase. In: Journal of the Textile Institute. 2005 ; Vol. 96, No. 2. pp. 109 - 116.
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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.",
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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, vol. 96, no. 2, pp. 109 - 116. https://doi.org/10.1533/joti.2004.0080

Enzymatic modification of wool with tyrosinase and peroxidase. / Lantto, Raija (Corresponding Author); Heine, E.; Freddi, G.; Lappalainen, Arja; Miettinen-Oinonen, Arja; Niku-Paavola, Marja-Leena; Buchert, Johanna.

In: Journal of the Textile Institute, Vol. 96, No. 2, 2005, p. 109 - 116.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Enzymatic modification of wool with tyrosinase and peroxidase

AU - Lantto, Raija

AU - Heine, E.

AU - Freddi, G.

AU - Lappalainen, Arja

AU - Miettinen-Oinonen, Arja

AU - Niku-Paavola, Marja-Leena

AU - Buchert, Johanna

PY - 2005

Y1 - 2005

N2 - 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.

AB - 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.

KW - proteinaceous fibre

KW - enzyme treatment

KW - cross-linking

KW - tyrosine

KW - peroxidase

KW - tyrosinase

U2 - 10.1533/joti.2004.0080

DO - 10.1533/joti.2004.0080

M3 - Article

VL - 96

SP - 109

EP - 116

JO - Journal of the Textile Institute

JF - Journal of the Textile Institute

SN - 0040-5000

IS - 2

ER -

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