Biodegradation of polycyclic aromatic hydrocarbons by a thermotolerant white rot fungus &lt;i&gt;Trametes polyzona&lt;/i&gt; RYNF13

Teerapatsakul, Churapa; Pothiratana, Chetsada; Chitradon, Lerluck; Thachepan, Surachai

doi:10.2323/jgam.2016.06.001

Cited by 19 publications

(11 citation statements)

References 46 publications

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“…ITS sequence of Pycnoporus cinnabarinus MUCL30555 and Ganoderma lucidum BRFM885 were used as the outgroup. The best phylogenetic tree was obtained using a maximum parsimony method (Figure 1(d)) Strain KU-RNW027 was clustered in the same position as T. polyzona RYNF13, voucher Cui8525, and WR710-1 [17,41].…”

Section: Resultsmentioning

confidence: 99%

“…These enzymes play significantly important roles in ligninolytic systems, fungal fruiting body formation, virulence factors of fungal pathogenicity, hyphal septa sealing, and pigmentation under stress responses [3–6]. Their abilities to oxidize a wide variety of recalcitrant aromatic compounds make MnP and laccase attractive candidates for eco-friendly applications including toxic aromatic dye decolorization [7,8], delignification and bleaching of pulp and paper [9], oxidative hair coloring [10], biocatalysts for material modification [11], wood protection [12], developing bactericidal paint [13], synthesis of iodinated phenolic compounds [14] and xenobiotic compounds degradation as pharmaceutical products [15,16], polycyclic aromatic hydrocarbons [17], fungal toxins [18], and pesticides [19].…”

Section: Introductionmentioning

confidence: 99%

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Morphological Characteristic Regulation of Ligninolytic Enzyme Produced by Trametes polyzona

2018

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A newly isolated white rot fungal strain KU-RNW027 was identified as Trametes polyzona, based on an analysis of its morphological characteristics and phylogenetic data. Aeration and fungal morphology were important factors which drove strain KU-RNW027 to secrete two different ligninolytic enzymes as manganese peroxidase (MnP) and laccase. Highest activities of MnP and laccase were obtained in a continuous shaking culture at 8 and 47 times higher, respectively, than under static conditions. Strain KU-RNW027 existed as pellets and free form mycelial clumps in submerged cultivation with the pellet form producing more enzymes. Fungal biomass increased with increasing amounts of pellet inoculum while pellet diameter decreased. Strain KU-RNW027 formed terminal chlamydospore-like structures in cultures inoculated with 0.05 g/L as optimal pellet inoculum which resulted in highest enzyme production. Enzyme production efficiency of T. polyzona KU-RNW027 depended on fungal pellet morphology as size, porosity, and formation of chlamydospore-like structures.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Morphological Characteristic Regulation of Ligninolytic Enzyme Produced by Trametes polyzona

2018

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“…Ligninolytic enzymes including manganese peroxidase (MnP), laccase, and lignin peroxidase (LiP), in particular from white rot fungi, have oxidizing abilities which make them attractive candidates for an eco-friendly approach to bioremediation of persistent phenolic and non-phenolic contaminants. [4][5][6][7][8]. Manganese peroxidase (EC 1.11.1.13, Mn(II): hydrogen-peroxide oxidoreductase) is a member of class II fungal secretion heme peroxidase in subfamily A.…”

Section: Introductionmentioning

confidence: 99%

Two Manganese Peroxidases and a Laccase ofTrametes polyzonaKU-RNW027 with Novel Properties for Dye and Pharmaceutical Product Degradation in Redox Mediator-Free System

et al. 2019

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Two manganese peroxidases (MnPs), MnP1 and MnP2, and a laccase, Lac1, were purified from Trametes polyzona KU-RNW027. Both MnPs showed high stability in organic solvents which triggered their activities. Metal ions activated both MnPs at certain concentrations. The two MnPs and Lac1, played important roles in dye degradation and pharmaceutical products deactivation in a redox mediator-free system. They completely degraded Remazol brilliant blue (25 mg/L) in 10-30 min and showed high degradation activities to Remazol navy blue and Remazol brilliant yellow, while Lac1 could remove 75% of Remazol red. These three purified enzymes effectively deactivated tetracycline, doxycycline, amoxicillin, and ciprofloxacin. Optimal reaction conditions were 50 C and pH 4.5. The two MnPs were activated by organic solvents and metal ions, indicating the efficacy of using T. polyzona KU-RNW027 for bioremediation of aromatic compounds in environments polluted with organic solvents and metal ions with no need for redox mediator supplements.

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“…Black poplar mushroom (A. cylindracea) was purchased from the Department of Agriculture (Bangkok, Thailand) and maintained on Potato Dextrose Agar (PDA) at room temperature (30 ± 2°C). Its identification was confirmed using PCR-based techniques as previously described (Teerapatsakul et al 2017) (using universal primers ITS1 and ITS4).…”

Section: Mushroommentioning

confidence: 99%

Putative hydrophobins of black poplar mushroom (Agrocybe cylindracea)

et al. 2020

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Hydrophobin proteins were extracted from Agrocybe cylindracea mycelia, the culture media (potato dextrose broth, PDB), and fruiting bodies. The putative hydrophobins obtained showed approximate sizes ranging from 8.0 to 25.0 kDa, dependent on their source. Multiple hydrophobin protein bands were detected in fruiting bodies. The hydrophobin yielded from aerial mycelia, or fruiting bodies, was approximately 6 mg/g dried weight. The crude extracts were examined for their properties in regards to surface modification, emulsification, and surface activity. Coating of hydrophobic Teflon sheet with crude extract made the surface significantly hydrophilic, whereas exposure of glass surfaces to extracts resulted in enhanced hydrophobicity. Crude extracts from culture media of A. cylindracea displayed emulsifying activity when mixed with hexane and could significantly reduce the surface tension of 60% ethanol and deionised water. The putative hydrophobin protein band from culture media (9.6 kDa), as analysed using LC-MS/MS, contained an amino acid fragment structurally similar to class I hydrophobin proteins from Basidiomycetes.

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Biodegradation of polycyclic aromatic hydrocarbons by a thermotolerant white rot fungus <i>Trametes polyzona</i> RYNF13

Cited by 19 publications

References 46 publications

Morphological Characteristic Regulation of Ligninolytic Enzyme Produced by Trametes polyzona

Morphological Characteristic Regulation of Ligninolytic Enzyme Produced by Trametes polyzona

Two Manganese Peroxidases and a Laccase ofTrametes polyzonaKU-RNW027 with Novel Properties for Dye and Pharmaceutical Product Degradation in Redox Mediator-Free System

Putative hydrophobins of black poplar mushroom (Agrocybe cylindracea)

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