Oxidation of peptides and proteins by Trichoderma reesei and Agaricus bisporus tyrosinases

Maija-Liisa Mattinen (Corresponding Author), Raija Lantto, Emilia Selinheimo, Kristiina Kruus, Johanna Buchert

Research output: Contribution to journalArticleScientificpeer-review

51 Citations (Scopus)

Abstract

The capability of a novel tyrosinase from Trichoderma reesei (TrTyr) to catalyse the oxidation and oxidative cross-linking of l-tyrosine (l-Y) and tyrosine side-chains in GYG and EGVYVHPV peptides, in bovine serum albumin (BSA) and β-casein proteins as well as in proteinaceous wool fibres was studied by oxygen consumption measurement, sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), reverse phase high-performance liquid chromatography (RP-HPLC), matrix assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS) and fluorescence microscopy. TrTyr was compared to the well-characterised tyrosinase from Agaricus bisporus (AbTyr) in terms of oxidation and cross-linking. According to the results obtained TrTyr was capable of cross-linking peptides and proteins more efficiently than AbTyr. However, the size and three-dimensional structure of the proteinaceous substrates proved to be crucial for the success of the enzymatic catalysis. Random coil β-casein could be cross-linked by TrTyr already in three hours, but large and compact BSA was not cross-linked even in 24 h. TrTyr could also be used to incorporate a diphenolic compound, l-dihydroxyphenyl alanine (l-dopa), into protein fibres whereas incorporation of a monophenol, l-Y was less efficient. Thus TrTyr is a potential tool for protein cross-linking and/or modification.
Original languageEnglish
Pages (from-to)395 - 402
Number of pages8
JournalJournal of Biotechnology
Volume133
DOIs
Publication statusPublished - 2008
MoE publication typeA1 Journal article-refereed

Keywords

  • Tyrosinase
  • Protein
  • Peptide
  • Tyrosine
  • Cross-linking
  • Grafting

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