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Characteristics And Use Of Multicopper Oxidases Enzymes

Aleksandra Góralczyk-Bińkowska
Aleksandra Góralczyk-Bińkowska
, 
Anna Jasińska
Anna Jasińska
 et 
Jerzy Długoński
Jerzy Długoński
   | 10 juin 2019
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Article Category: article
Publié en ligne: 10 juin 2019
Pages: 7 - 18
Reçu: 01 juin 2018
Accepté: 01 nov. 2018
DOI: https://doi.org/10.21307/PM-2019.58.1.007
© 2019 Aleksandra Góralczyk-Bińkowska et al., published by Sciendo
This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.

Fig. 1.

Model of the catalytic cluster of MCO.
Model of the catalytic cluster of MCO.

Fig. 2.

Schematic of the catalytic mechanism of laccase.
Schematic of the catalytic mechanism of laccase.

Fig 3.

Mechanisms of reactions catalyzed by MCO. I – reactions occurring directly, II – reactions occurring in the presence of a mediator, III – coupling reactions [Polak i Jarosz-Wilkołaka [66], modified].
Mechanisms of reactions catalyzed by MCO. I – reactions occurring directly, II – reactions occurring in the presence of a mediator, III – coupling reactions [Polak i Jarosz-Wilkołaka [66], modified].

Fig. 4.

The proposed scheme for the differentiation of laccases from other ligninolitic enzymes. According to Fernandes et al. [18], modified.
The proposed scheme for the differentiation of laccases from other ligninolitic enzymes. According to Fernandes et al. [18], modified.

Classification of multicopper oxidases

Group of MCOs Microorganism Enzyme characteristic References
Basidomycota laccases Trametes pubescens pH 3–4.5; DMP, syringaldazine [21]
Ascomycota MCOs Aspergillus niger pH 5–6; DMPPDA [90]
Insects laccases Anopheles gambiae pH 6; ABTS [46]
Fungal pigments MCOs Aspergillus niger pH 5; DMPPDA [90]
Fungal ferroxidases (Fet3p) Saccharomyces cerevisiae pH 5; p-phenylendiamine [86]
Ascorbate oxidases Brassica oleracea var. italica pH 7 ascorbic acid solution [80]
Plants laccases Rhus vernicifera pH 9; syringaldazine [96]
Bilirubin oxidases Myrothecium verrucaria pH 8; syringaldazine [96]
Copper efflux proteins (CueO) Escherichia coli pH 6.5; DMP [72]
Bacterial laccases (CotA) Bacillus subtilis T ½ in 80°C after 2–4 h [61]
Copper-resistance proteins (CopA) Pseudomonas syringae pH 5; DMP [84]

Reactions of synthesis, detection and biodegradation catalyzed by enzymes from the MCOs group

Application Enzyme, activity Organism Substrate, catalyzed reaction Reaction conditions, process efficiency References
Biodegradation of xenobiotics Multicopper oxidase (1.5 U/mL) Spirulina platensis CFTRI Reactive Blue 4 (100 mg/L) 96%; 4 h [1]
Laccase Pleurotus ostreatus Atrazine, pentachlorophenol, naproxen, oksybenzone (0.5 mg/L) 60–99%; 24 h; vanillin [3]
Bilirubin oxidase Magnaporthe oryzae Remazol Brilliant Blue R (80 mg/L) 95%; 20 min.; ABTS [14]
Laccase cocktail (100 U/L) Pycnoporus sanguineus CS43 Bisphenol A, 4-nonylphenol, tricolsan (10 mg/L) 89–100%; 5 h [22]
Laccase (3 U/mL) Phoma sp. UHH 5-1-03 Sulfamethoxazole (0.25 mM) 87%; 22 h [27]
Laccase (0.05 U/mL) T. versicolor Chloropyrifos, atrazine, chlorothalonil, pyrimethanil (20 mg/L) 90–100%; 24 h – 8 days [38]
Bilirubin oxidase Myrothecium sp. IMER1 Remazol Brilliant Blue R (80 mg/L) 91, 5%; 25 min.; ABTS [48]
Laccase-like multicopper oxidase (2 U/mL) Streptomyces sp. C1 Indigo Carmine, Diamond Black PV 56–84%; 2 h; syringaldehyde [49]
Laccase (100 U/L) Pycnoporus sanguineus CS43 2,4-dichlorophenol, β-nonylphenol (10 mg/L) 71–97%; 8 h [75]
Immobilized laccase (1 U/mL) Trametes pubescens Cui 7571 Acid Black 172 (50 mg/L) 69%; 48 h [100]
Synthesis and polymerization reactions Laccase Trametes versicolor 4-methyl-3-hydroxyanthranilic acid Actinocin syntesis, pH 5, immobilization in polyacrylamide gel [63]
Laccase Myceliophthora thermophila methyl-1,4-hydroquinone, 2,3-dimethyl-1,4-hydroquinone Synthesis of β-lactam antibiotics [56]
Laccase (350 U/mg) Coriolus hirsutus Aniline (50 mM) Polymerization of vanillin in lignosulfonate complex at pH 3.5–4.4 [42]
Laccase Trametes pusbescens Biosynthesis of totarol dimers 62.6% conversion of totarol after 24 h; pH 4.5–5, 30°C [62]
Detection reactions Lacasse (0.29 U/mL) Aspergillus oryzae Detection of luteolin Immobilized in chitosan (Chi) chemically cross-linked; with cyanuric chloride (CC) [20]
Laccase cocktail (31.5 U/mL) Pleurotus ostreatus Detection of adrenaline and dopamine Adsorption on carbon paste; pH 7.0 [47]
Bilirubin oxidase (50 U) Myrothecium verrucaria Detection of bilirubin Immobilization in gold nanoparticles, pH 8.4 [41]
Glucose dehydrogenase and laccase complex Coriolus hirsutus Detection of morphine Immobilization in polyvinylalcohol (PVA); pH 6.5 [5]
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