Characterization of two new multiforms of Trametes pubescens laccase

Shleev, Sergey; Nikitina, O. V.; Christenson, Andreas; Reimann, C.T.; Yaropolov, A. I.; Ruzgas, Tautgirdas; Gorton, Lo

doi:10.1016/j.bioorg.2006.08.001

Cited by 39 publications

(14 citation statements)

References 59 publications

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“…The four Cu ions are classified into three different types, depending on their optical and magnetic properties (Sakurai and Kataoka 2007;Solomon et al 1996) Laccases, which belong to the MCO family, is the most studied MCO because of its use in numerous biotechnological applications ranging from pulp bleaching, decolorization of dye, polymer synthesis to detoxification, and bioremediation (Mayer and Staples 2002). For more than 30 years, (Tarasevich et al 1979), the four-electron reduction of O 2 to water under physiological conditions by laccases has also been investigated (Ackermann et al 2010; Barriere et al 2006; Barton et al 2002;Gallaway et al 2008;Mano et al 2006;Rowinski et al 2004;Shleev et al 2007). This is one of the most extensively studied electrochemical reactions because miniature biofuel cell with O 2 -reducing cathode and glucose-oxidizing anodes may power, in the near future, implanted medical devices (Barton et al 2004;Boland and Leech 2012;Falk et al 2012;Gao et al 2010;Halamkova et al 2012;Kamitaka et al 2007b;Karaskiewicz et al 2012;Leech et al 2012;Rasmussen et al 2012;Tasca et al 2010;Zebda et al 2011).…”

Section: Introductionmentioning

confidence: 99%

Features and applications of bilirubin oxidases

Mano

2012

Appl Microbiol Biotechnol

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Discovered in 1981 by Tanaka and Murao (Agric Biol Chem 45:2383-2384, 1981), bilirubin oxidase (BOD) is a sub-group of multicopper oxidases (MCOs) also utilizing four Cu(+/2+) ions. It catalyzes the oxidation of bilirubin to biliverdin, hence the classification of bilirubin oxidase, and has been primarily used in the determination of bilirubin in serum and thereby in the diagnostic of jaundice. Unlike laccases, the most studied MCOs, BODs display a high activity and stability at neutral pH, a high tolerance towards chloride anions and other chelators, and for some species, a high thermal tolerance. Therefore, BODs could potentially be an alternative to laccase which are so far mainly restricted to applications in acid media. Because of growing interest in BODs for numerous applications under mild pH conditions, based on the number of patents and publications published in the last 5 years, here I will summarize the available data on the biochemical properties of BODs, their occurrence, and their possible biotechnological use in (1) the field of Healthcare for the elaboration of biofuel cells or bilirubin sensors or (2) the field of environmentally desirable applications such as depollution, decolorization of dyes, and pulp bleaching.

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Section: Introductionmentioning

confidence: 99%

Features and applications of bilirubin oxidases

Mano

2012

Appl Microbiol Biotechnol

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“…The presence of different genes encoding laccase isozymes in Ganoderma strains may have an adaptive value for these WRF that grow on complex substrates such as hard wood, and also in changing environments (Luis et al, 2004; Shleev et al, 2007; Majeau et al, 2010) such as the urban ecosystems from where they were isolated. The presence of these laccase isozymes together with the peroxidases described in this study could provide to these strains multiple advantages to survive in their natural habitats, but might also be valuable for the degradation of a variety of recalcitrant environmental pollutants such as POPs.…”

Section: Discussionmentioning

confidence: 99%

Diversity of Ligninolytic Enzymes and Their Genes in Strains of the Genus Ganoderma: Applicable for Biodegradation of Xenobiotic Compounds?

Torres-Farradá

León²,

Rineau

et al. 2017

Front. Microbiol.

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White-rot fungi (WRF) and their ligninolytic enzymes (laccases and peroxidases) are considered promising biotechnological tools to remove lignin related Persistent Organic Pollutants from industrial wastewaters and contaminated ecosystems. A high diversity of the genus Ganoderma has been reported in Cuba; in spite of this, the diversity of ligninolytic enzymes and their genes remained unexplored. In this study, 13 native WRF strains were isolated from decayed wood in urban ecosystems in Havana (Cuba). All strains were identified as Ganoderma sp. using a multiplex polymerase chain reaction (PCR)-method based on ITS sequences. All Ganoderma sp. strains produced laccase enzymes at higher levels than non-specific peroxidases. Native-PAGE of extracellular enzymatic extracts revealed a high diversity of laccase isozymes patterns between the strains, suggesting the presence of different amino acid sequences in the laccase enzymes produced by these Ganoderma strains. We determined the diversity of genes encoding laccases and peroxidases using a PCR and cloning approach with basidiomycete-specific primers. Between two and five laccase genes were detected in each strain. In contrast, only one gene encoding manganese peroxidase or versatile peroxidase was detected in each strain. The translated laccases and peroxidases amino acid sequences have not been described before. Extracellular crude enzymatic extracts produced by the Ganoderma UH strains, were able to degrade model chromophoric compounds such as anthraquinone and azo dyes. These findings hold promises for the development of a practical application for the treatment of textile industry wastewaters and also for bioremediation of polluted ecosystems by well-adapted native WRF strains.

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“…A thermo stable, metal-tolerant laccase is reportedly produced by marine-derived fungi, Cerrena unicolor 96 . Various researchers have isolated laccase producing fungi from different sources including Trichoderma harzianum 97 , Trichoderma atroviride 98 and Trichoderma longibrachiatum 99 , Trametes versicolor 100 , Lentinus tigrinus 101 , Trametes pubescens 102 , Cyathus bulleri 103 , Paecilomyces sp. 104 , P. chrysosporium 105 , Lentines edodes 106 and Pleurotus ostreatus 107,81 , Ganoderma lucidum 91 , Alternaria tenuissima 108 and Trichoderma sp.…”

Section: Laccasementioning

confidence: 99%

"Lignocellulose Degrading Enzymes from Fungi and Their Industrial Applications"

2017

IJCRR

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The rich diversity of fungi and diverse range of enzymes produced by them together make researchers to exploit their potential for various industrial applications. Few of the fungal enzymes have already been harnessed and many other are to be explored and brought into use. Recent studies suggested that the lignin degrading fungi can be used in the bioremediation of aromatic hydrocarbons including dioxins, dibenzofuran, aromatic dyes, etc. Employing fungal enzymes for the treatment of pollutants has gained attraction recent days for their selectivity, specificity and eco-friendly nature. Of these enzymes, peroxidases (lignin peroxidase and manganese peroxidase) and laccases are the two major classes of enzymes involved in biodegradation of lignin and recalcitrant xenobiotics. In addition, cellulase and hemicellulase were found to play a role in the management of lignocellulosic wastes. The present review gives a detailed account on the various lignocelluloses degrading enzymes, their fungal sources and their industrial applications.

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Characterization of two new multiforms of Trametes pubescens laccase

Cited by 39 publications

References 59 publications

Features and applications of bilirubin oxidases

Features and applications of bilirubin oxidases

Diversity of Ligninolytic Enzymes and Their Genes in Strains of the Genus Ganoderma: Applicable for Biodegradation of Xenobiotic Compounds?

"Lignocellulose Degrading Enzymes from Fungi and Their Industrial Applications"

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