Bacterial tyrosinases and their applications

G. Faccio, Kristiina Kruus, Markku Saloheimo, L. Thöny-Meyer (Corresponding Author)

Research output: Contribution to journalReview ArticleScientificpeer-review

45 Citations (Scopus)

Abstract

Tyrosinases with different physico-chemical properties have been identified from various bacterial phyla such as Actinobacteria and Proteobacteria and their production is often inducible by environmental stresses. Tyrosinases are enzymes catalysing the oxidation of mono- and di-phenolic compounds to corresponding quinones with the concomitant reduction of molecular oxygen to water. Since the quinone produced can further react non-enzymatically with other nucleophiles, e.g. amino groups, many tyrosinases have a recorded cross-linking activity on proteins. Various bacterial tyrosinases oxidise tyrosine, catechol, l/d-DOPA, caffeic acid and polyphenolic substrates such as catechins. This substrate specificity has been exploited to engineer biosensors able to detect even minimal amounts of different phenolic compounds. The physiological role of tyrosinases in the biosynthesis of melanins has been used for the production of coloured and dyeing agents. Moreover, the cross-linking activity of tyrosinases has found application in food processing and in the functionalisation of materials. Numerous tyrosinases with varying substrate specificities and stability features have been isolated from bacteria and they can constitute valuable alternatives to the well-studied tyrosinase from common mushroom.
Original languageEnglish
Pages (from-to)1749-1760
Number of pages11
JournalProcess Biochemistry
Volume47
Issue number12
DOIs
Publication statusPublished - 2012
MoE publication typeA2 Review article in a scientific journal

Fingerprint

Monophenol Monooxygenase
Substrates
Melanin
Food processing
Nucleophiles
Molecular oxygen
Biosynthesis
Biosensors
Dyeing
Chemical properties
Bacteria
Enzymes
Substrate Specificity
Proteins
Engineers
Oxidation
Acids
Proteobacteria
Quinones
Food Handling

Keywords

  • Bioremediation
  • biosensors
  • biosynthesis
  • dyeing
  • food
  • tyrosinase

Cite this

Faccio, G. ; Kruus, Kristiina ; Saloheimo, Markku ; Thöny-Meyer, L. / Bacterial tyrosinases and their applications. In: Process Biochemistry. 2012 ; Vol. 47, No. 12. pp. 1749-1760.
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Bacterial tyrosinases and their applications. / Faccio, G.; Kruus, Kristiina; Saloheimo, Markku; Thöny-Meyer, L. (Corresponding Author).

In: Process Biochemistry, Vol. 47, No. 12, 2012, p. 1749-1760.

Research output: Contribution to journalReview ArticleScientificpeer-review

TY - JOUR

T1 - Bacterial tyrosinases and their applications

AU - Faccio, G.

AU - Kruus, Kristiina

AU - Saloheimo, Markku

AU - Thöny-Meyer, L.

PY - 2012

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N2 - Tyrosinases with different physico-chemical properties have been identified from various bacterial phyla such as Actinobacteria and Proteobacteria and their production is often inducible by environmental stresses. Tyrosinases are enzymes catalysing the oxidation of mono- and di-phenolic compounds to corresponding quinones with the concomitant reduction of molecular oxygen to water. Since the quinone produced can further react non-enzymatically with other nucleophiles, e.g. amino groups, many tyrosinases have a recorded cross-linking activity on proteins. Various bacterial tyrosinases oxidise tyrosine, catechol, l/d-DOPA, caffeic acid and polyphenolic substrates such as catechins. This substrate specificity has been exploited to engineer biosensors able to detect even minimal amounts of different phenolic compounds. The physiological role of tyrosinases in the biosynthesis of melanins has been used for the production of coloured and dyeing agents. Moreover, the cross-linking activity of tyrosinases has found application in food processing and in the functionalisation of materials. Numerous tyrosinases with varying substrate specificities and stability features have been isolated from bacteria and they can constitute valuable alternatives to the well-studied tyrosinase from common mushroom.

AB - Tyrosinases with different physico-chemical properties have been identified from various bacterial phyla such as Actinobacteria and Proteobacteria and their production is often inducible by environmental stresses. Tyrosinases are enzymes catalysing the oxidation of mono- and di-phenolic compounds to corresponding quinones with the concomitant reduction of molecular oxygen to water. Since the quinone produced can further react non-enzymatically with other nucleophiles, e.g. amino groups, many tyrosinases have a recorded cross-linking activity on proteins. Various bacterial tyrosinases oxidise tyrosine, catechol, l/d-DOPA, caffeic acid and polyphenolic substrates such as catechins. This substrate specificity has been exploited to engineer biosensors able to detect even minimal amounts of different phenolic compounds. The physiological role of tyrosinases in the biosynthesis of melanins has been used for the production of coloured and dyeing agents. Moreover, the cross-linking activity of tyrosinases has found application in food processing and in the functionalisation of materials. Numerous tyrosinases with varying substrate specificities and stability features have been isolated from bacteria and they can constitute valuable alternatives to the well-studied tyrosinase from common mushroom.

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KW - biosynthesis

KW - dyeing

KW - food

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