Comparison of the characteristics of fungal and plant tyrosinases

Emilia Selinheimo, Deirdre NiEidhin, Charlotte Steffensen, Jacob Nielsen, Anne Lomascolo, Sonia Halaouli, Eric Record, David O’Beirne, Johanna Buchert, Kristiina Kruus

Research output: Contribution to journalArticleScientificpeer-review

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Abstract

Enzymatic crosslinking provides valuable means for modifying functionality and structural properties of different polymers. Tyrosinases catalyze the hydroxylation of various monophenols to the corresponding o-diphenols, and the subsequent oxidation of o-diphenols to the corresponding quinones, which are highly reactive and can further undergo non-enzymatic reactions to produce mixed melanins and heterogeneous polymers. Tyrosinases are also capable of oxidizing protein- and peptide-bound tyrosyl residues, resulting in the formation of inter- and intra-molecular crosslinks.
Tyrosinases from apple (AT), potato (PT), the white rot fungus Pycnoporus sanguineus (PsT), the filamentous fungus Trichoderma reesei (TrT) and the edible mushroom Agaricus bisporus (AbT) were compared for their biochemical characteristics.
The enzymes showed different features in terms of substrate specificity, stereo-specificity, inhibition, and ability to crosslink the model protein, α-casein. All enzymes were found to produce identical semiquinone radicals from the substrates as analyzed by electron spin resonance spectroscopy. The result suggests similar reaction mechanism between the tyrosinases. PsT enzyme had the highest monophenolase/diphenolase ratio for the oxidation of monophenolic l-tyrosine and diphenolic l-dopa, although the tyrosinases generally had noticeably lower activity on monophenols than on di- or triphenols.
The activity of AT and PT on tyrosine was particularly low, which largely explains the poor crosslinking ability of the model protein α-casein by these enzymes. AbT oxidized peptide-bound tyrosine, but was not able to crosslink α-casein. Conversely, the activity of PsT on model peptides was relatively low, although the enzyme could crosslink α-casein. In the reaction conditions studied, TrT showed the best ability to crosslink α-casein.
TrT also had the highest activity on most of the tested monophenols, and showed noticeable short lag periods prior to the oxidation.
Original languageEnglish
Pages (from-to)471-480
JournalJournal of Biotechnology
Volume130
Issue number4
DOIs
Publication statusPublished - 2007
MoE publication typeA1 Journal article-refereed

Fingerprint

Casein
Monophenol Monooxygenase
Caseins
Enzymes
Peptides
Tyrosine
Solanum tuberosum
Fungi
Proteins
Crosslinking
Oxidation
Pycnoporus
Polymers
Melanin
Electron spin resonance spectroscopy
Agaricus
Quinones
Hydroxylation
Dihydroxyphenylalanine
Trichoderma

Keywords

  • Tyrosinase
  • Plant
  • Fungal
  • Specificity
  • Inhibition
  • Crosslinking

Cite this

Selinheimo, E., NiEidhin, D., Steffensen, C., Nielsen, J., Lomascolo, A., Halaouli, S., ... Kruus, K. (2007). Comparison of the characteristics of fungal and plant tyrosinases. Journal of Biotechnology, 130(4), 471-480. https://doi.org/10.1016/j.jbiotec.2007.05.018
Selinheimo, Emilia ; NiEidhin, Deirdre ; Steffensen, Charlotte ; Nielsen, Jacob ; Lomascolo, Anne ; Halaouli, Sonia ; Record, Eric ; O’Beirne, David ; Buchert, Johanna ; Kruus, Kristiina. / Comparison of the characteristics of fungal and plant tyrosinases. In: Journal of Biotechnology. 2007 ; Vol. 130, No. 4. pp. 471-480.
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Selinheimo, E, NiEidhin, D, Steffensen, C, Nielsen, J, Lomascolo, A, Halaouli, S, Record, E, O’Beirne, D, Buchert, J & Kruus, K 2007, 'Comparison of the characteristics of fungal and plant tyrosinases', Journal of Biotechnology, vol. 130, no. 4, pp. 471-480. https://doi.org/10.1016/j.jbiotec.2007.05.018

Comparison of the characteristics of fungal and plant tyrosinases. / Selinheimo, Emilia; NiEidhin, Deirdre; Steffensen, Charlotte; Nielsen, Jacob; Lomascolo, Anne; Halaouli, Sonia; Record, Eric; O’Beirne, David; Buchert, Johanna; Kruus, Kristiina.

In: Journal of Biotechnology, Vol. 130, No. 4, 2007, p. 471-480.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Comparison of the characteristics of fungal and plant tyrosinases

AU - Selinheimo, Emilia

AU - NiEidhin, Deirdre

AU - Steffensen, Charlotte

AU - Nielsen, Jacob

AU - Lomascolo, Anne

AU - Halaouli, Sonia

AU - Record, Eric

AU - O’Beirne, David

AU - Buchert, Johanna

AU - Kruus, Kristiina

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N2 - Enzymatic crosslinking provides valuable means for modifying functionality and structural properties of different polymers. Tyrosinases catalyze the hydroxylation of various monophenols to the corresponding o-diphenols, and the subsequent oxidation of o-diphenols to the corresponding quinones, which are highly reactive and can further undergo non-enzymatic reactions to produce mixed melanins and heterogeneous polymers. Tyrosinases are also capable of oxidizing protein- and peptide-bound tyrosyl residues, resulting in the formation of inter- and intra-molecular crosslinks. Tyrosinases from apple (AT), potato (PT), the white rot fungus Pycnoporus sanguineus (PsT), the filamentous fungus Trichoderma reesei (TrT) and the edible mushroom Agaricus bisporus (AbT) were compared for their biochemical characteristics. The enzymes showed different features in terms of substrate specificity, stereo-specificity, inhibition, and ability to crosslink the model protein, α-casein. All enzymes were found to produce identical semiquinone radicals from the substrates as analyzed by electron spin resonance spectroscopy. The result suggests similar reaction mechanism between the tyrosinases. PsT enzyme had the highest monophenolase/diphenolase ratio for the oxidation of monophenolic l-tyrosine and diphenolic l-dopa, although the tyrosinases generally had noticeably lower activity on monophenols than on di- or triphenols. The activity of AT and PT on tyrosine was particularly low, which largely explains the poor crosslinking ability of the model protein α-casein by these enzymes. AbT oxidized peptide-bound tyrosine, but was not able to crosslink α-casein. Conversely, the activity of PsT on model peptides was relatively low, although the enzyme could crosslink α-casein. In the reaction conditions studied, TrT showed the best ability to crosslink α-casein. TrT also had the highest activity on most of the tested monophenols, and showed noticeable short lag periods prior to the oxidation.

AB - Enzymatic crosslinking provides valuable means for modifying functionality and structural properties of different polymers. Tyrosinases catalyze the hydroxylation of various monophenols to the corresponding o-diphenols, and the subsequent oxidation of o-diphenols to the corresponding quinones, which are highly reactive and can further undergo non-enzymatic reactions to produce mixed melanins and heterogeneous polymers. Tyrosinases are also capable of oxidizing protein- and peptide-bound tyrosyl residues, resulting in the formation of inter- and intra-molecular crosslinks. Tyrosinases from apple (AT), potato (PT), the white rot fungus Pycnoporus sanguineus (PsT), the filamentous fungus Trichoderma reesei (TrT) and the edible mushroom Agaricus bisporus (AbT) were compared for their biochemical characteristics. The enzymes showed different features in terms of substrate specificity, stereo-specificity, inhibition, and ability to crosslink the model protein, α-casein. All enzymes were found to produce identical semiquinone radicals from the substrates as analyzed by electron spin resonance spectroscopy. The result suggests similar reaction mechanism between the tyrosinases. PsT enzyme had the highest monophenolase/diphenolase ratio for the oxidation of monophenolic l-tyrosine and diphenolic l-dopa, although the tyrosinases generally had noticeably lower activity on monophenols than on di- or triphenols. The activity of AT and PT on tyrosine was particularly low, which largely explains the poor crosslinking ability of the model protein α-casein by these enzymes. AbT oxidized peptide-bound tyrosine, but was not able to crosslink α-casein. Conversely, the activity of PsT on model peptides was relatively low, although the enzyme could crosslink α-casein. In the reaction conditions studied, TrT showed the best ability to crosslink α-casein. TrT also had the highest activity on most of the tested monophenols, and showed noticeable short lag periods prior to the oxidation.

KW - Tyrosinase

KW - Plant

KW - Fungal

KW - Specificity

KW - Inhibition

KW - Crosslinking

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DO - 10.1016/j.jbiotec.2007.05.018

M3 - Article

VL - 130

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JO - Journal of Biotechnology

JF - Journal of Biotechnology

SN - 0168-1656

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Selinheimo E, NiEidhin D, Steffensen C, Nielsen J, Lomascolo A, Halaouli S et al. Comparison of the characteristics of fungal and plant tyrosinases. Journal of Biotechnology. 2007;130(4):471-480. https://doi.org/10.1016/j.jbiotec.2007.05.018