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

50 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

Fingerprint

Agaricus
Trichoderma
Monophenol Monooxygenase
Peptides
Proteins
Tyrosine
Casein
Oxidation
Bovine Serum Albumin
Caseins
Wool fibers
Wool
Fluorescence microscopy
High performance liquid chromatography
Sodium dodecyl sulfate
Reverse-Phase Chromatography
Polyacrylates
Electrophoresis
Catalysis
Fluorescence Microscopy

Keywords

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

Cite this

Mattinen, Maija-Liisa ; Lantto, Raija ; Selinheimo, Emilia ; Kruus, Kristiina ; Buchert, Johanna. / Oxidation of peptides and proteins by Trichoderma reesei and Agaricus bisporus tyrosinases. In: Journal of Biotechnology. 2008 ; Vol. 133. pp. 395 - 402.
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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.",
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author = "Maija-Liisa Mattinen and Raija Lantto and Emilia Selinheimo and Kristiina Kruus and Johanna Buchert",
year = "2008",
doi = "10.1016/j.jbiotec.2007.10.009",
language = "English",
volume = "133",
pages = "395 -- 402",
journal = "Journal of Biotechnology",
issn = "0168-1656",
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Oxidation of peptides and proteins by Trichoderma reesei and Agaricus bisporus tyrosinases. / Mattinen, Maija-Liisa (Corresponding Author); Lantto, Raija; Selinheimo, Emilia; Kruus, Kristiina; Buchert, Johanna.

In: Journal of Biotechnology, Vol. 133, 2008, p. 395 - 402.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Oxidation of peptides and proteins by Trichoderma reesei and Agaricus bisporus tyrosinases

AU - Mattinen, Maija-Liisa

AU - Lantto, Raija

AU - Selinheimo, Emilia

AU - Kruus, Kristiina

AU - Buchert, Johanna

PY - 2008

Y1 - 2008

N2 - 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.

AB - 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.

KW - Tyrosinase

KW - Protein

KW - Peptide

KW - Tyrosine

KW - Cross-linking

KW - Grafting

U2 - 10.1016/j.jbiotec.2007.10.009

DO - 10.1016/j.jbiotec.2007.10.009

M3 - Article

VL - 133

SP - 395

EP - 402

JO - Journal of Biotechnology

JF - Journal of Biotechnology

SN - 0168-1656

ER -