Laccase produced by a thermotolerant strain of Trametes trogii LK13

Yan, Jinping; Chen, Yuhui; Niu, Jiezhen; Chen, Daidi; Irbis, Chagan

doi:10.1590/s1517-838246120130895

Cited by 20 publications

(12 citation statements)

References 29 publications

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“…The tolerance of Lac 37 II to acetonitrile and ethanol in this study were similar to that of laccase-like enzyme from the marine sediment samples (Yang et al, 2018). The promotive effect of acetonitrile on laccase activity has been confirmed for the crude laccase of T. trogii LK13 (Yan et al, 2015). In addition, methanol at concentrations ranging from 1 to 5% (v/v) slightly lowered activity by 11.7-16.3%, and 10% ethanol (v/v) led to a 56.1% loss of activity.…”

Section: Effect Of Organic Solvents On Activity Of Lac 37 IIsupporting

confidence: 76%

A Thermo-Active Laccase Isoenzyme From Trametes trogii and Its Potential for Dye Decolorization at High Temperature

Yang

et al. 2020

Front. Microbiol.

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A thermo-activation and thermostable laccase isoenzyme (Lac 37 II) produced by Trametes trogii S0301 at 37 • C was purified to apparent homogeneity by anionic exchange chromatography and sephadex G-75 chromatography, with 12.3% of yeiled and a specific activity of 343.1 U mg −1 . The molecular weight of the purified Lac 37 II was estimated to be approximately 56 kDa in 12% sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The optimal pH and temperature for the protein was 2.7 and 60 • C, respectively. The purified Lac 37 II showed higher resistance to all tested metal ions and organic solvents except for Fe 2+ and Cd 2+ at 37 • C and the activity of the purified Lac 37 was significantly enhanced by Cu 2+ at 50 mM. The K cat , K m , and K cat /K m of Lac 37 II were 2.977 s −1 , 16.1 µM, and 184.9 s −1 µM −1 , respecively, in the condition of pH 2.7 and 60 • C using ABTS as a substrate. Peptide-mass fingerprinting analysis showed that the Lac 37 II matched to the gene-deduced sequences of lcc3 in T. trogii BAFC 463, other than Lcc1, Lcc 2, and Lcc 4. Compared with laccase prepared at 28 • C, the onset of thermo-activation of Lac 37 II activity occurred at 30 • C with an increase of 10%, and reached its maximum at the temperatures range of 40-60 • C with an increase of about 40% of their original activity. Furthermore, Lac 37 II showed the efficient decolorization ability toward triphenylmethane dyes at 60 • C, with decolorization rates of 100 and 99.1% for 25 mg L −1 malachite and crystal violet in 5 h, respectively, when hydroxybenzotriazole (HBT) was used as a mediator. In conclusion, it is the first time to report a thermoactivation laccase from a thermophilic T. trogii strain, which has a better enzyme property and higher decolorization ability among fungal laccases, and it also has a further application prospective in the field of biotechnology.

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Section: Effect Of Organic Solvents On Activity Of Lac 37 IIsupporting

confidence: 76%

A Thermo-Active Laccase Isoenzyme From Trametes trogii and Its Potential for Dye Decolorization at High Temperature

Yang

et al. 2020

Front. Microbiol.

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“…Previous studies have shown that a laccase from Physisporinus rivulosus remained stable at 50°C with optimal activity at pH 3.5 (69). Similarly, a laccase from Trametes trogii was shown to sustain temperatures up to 75°C, although only for short 5-min incubations (70). Nevertheless, our results suggest that the laccase activity from the D. pusillus LMB4 extract has higher tolerance to acidic and thermally induced perturbations than previously identified fungal laccases.…”

Section: Effect Of Ph and Temperature On The Enzymatic Extracts Obtaicontrasting

confidence: 48%

Genome sequencing and functional characterization of aDictyopanus pusillusfungal extract offers a promising alternative for lignocellulose pretreatment of oil palm residues

Rueda

Santos

Vincent

et al. 2019

Preprint

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The pretreatment of biomass is a critical requirement of bio-renewable fuel production from lignocellulose. Although current processes primarily involve chemical and physical approaches, the biological breakdown of lignin using enzymes and microorganisms is quickly becoming an interesting ecofriendly alternative to classical processes. As a result, bioprospection of wild fungi from naturally occurring lignin-rich sources remains a suitable method to uncover and isolate new species exhibiting ligninolytic activity. In this study, wild species of white rot fungi were collected from Colombian forests based on their natural wood decay ability and high capacity to secrete oxidoreductases with high affinity for phenolic polymers such as lignin. Based on high activity obtained from solid-state fermentation using a lignocellulose source from oil palm as matrix, we describe the isolation and whole-genome sequencing of Dictyopanus pusillus, a wild basidiomycete fungus exhibiting ABTS oxidation as an indication of laccase activity. Functional characterization of a crude enzymatic extract identified laccase activity as the main enzymatic contributor to fungal extracts, an observation supported by the identification of 13 putative genes encoding for homologous laccases in the genome. To the best of our knowledge, this represents the first report of an enzymatic extract exhibiting laccase activity in the Dictyopanus genera, offering means to exploit this species and its enzymes for the delignification process of lignocellulosic by-products from oil palm.

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“…Previous studies have shown that a laccase from Physisporinus rivulosus remained stable at 50°C with optimal activity at pH 3.5 [ 70 ]. Similarly, a laccase from Trametes trogii was shown to sustain temperatures up to 75°C, although only for short 5-min incubations [ 71 ]. Nevertheless, our results suggest that the laccase activity from the D .…”

Section: Resultsmentioning

confidence: 99%

Genome sequencing and functional characterization of a Dictyopanus pusillus fungal enzymatic extract offers a promising alternative for lignocellulose pretreatment of oil palm residues

et al. 2020

View full text Add to dashboard Cite

The pretreatment of biomass remains a critical requirement for bio-renewable fuel production from lignocellulose. Although current processes primarily involve chemical and physical approaches, the biological breakdown of lignin using enzymes and microorganisms is quickly becoming an interesting eco-friendly alternative to classical processes. As a result, bioprospection of wild fungi from naturally occurring lignin-rich sources remains a suitable method to uncover and isolate new species exhibiting ligninolytic activity. In this study, wild species of white rot fungi were collected from Colombian forests based on their natural wood decay ability and high capacity to secrete oxidoreductases with high affinity for phenolic polymers such as lignin. Based on high activity obtained from solid-state fermentation using a lignocellulose source from oil palm as matrix, we describe the isolation and wholegenome sequencing of Dictyopanus pusillus, a wild basidiomycete fungus exhibiting ABTS oxidation as an indication of laccase activity. Functional characterization of a crude enzymatic extract identified laccase activity as the main enzymatic contributor to fungal extracts, an observation supported by the identification of 13 putative genes encoding for homologous laccases in the genome. To the best of our knowledge, this represents the first report of an enzymatic extract exhibiting laccase activity in the Dictyopanus genera, offering means to exploit this species and its enzymes for the delignification process of lignocellulosic by-products from oil palm.

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Laccase produced by a thermotolerant strain of Trametes trogii LK13

Cited by 20 publications

References 29 publications

A Thermo-Active Laccase Isoenzyme From Trametes trogii and Its Potential for Dye Decolorization at High Temperature

A Thermo-Active Laccase Isoenzyme From Trametes trogii and Its Potential for Dye Decolorization at High Temperature

Genome sequencing and functional characterization of aDictyopanus pusillusfungal extract offers a promising alternative for lignocellulose pretreatment of oil palm residues

Genome sequencing and functional characterization of a Dictyopanus pusillus fungal enzymatic extract offers a promising alternative for lignocellulose pretreatment of oil palm residues

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