Purification and characterization of an extracellular laccase from the edible mushroom Lentinula edodes , and decolorization of chemically different dyes

Nagai, Masaru; Sato, Toshitsugu; Watanabe, Hisayuki; Saito, Kumiko; Kawata, Maki; Enei, Hitoshi

doi:10.1007/s00253-002-1109-2

Cited by 232 publications

(29 citation statements)

References 36 publications

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“…5), similar to other laccases from Lentinus tigrinus (60 °C) (Xu and Wang 2012), Tricholoma matsutake (60 °C) (Lijing et al 2015), Ganoderma lucidum (60 °C) (Wang and Ng 2006a), Clitocybe maxima (60 °C) (Zhang et al 2010), Hericium erinaceus (40 °C) (Wang and Ng 2004) and Lentinula edodes (40 °C) (Nagai et al 2002). Chaurasia et al (2013a, b) have reported the maximum laccase activity at 40 °C.…”

Section: Resultssupporting

confidence: 55%

Purification and characterization of laccase from Marasmius species BBKAV79 and effective decolorization of selected textile dyes

Vantamuri

Kaliwal

2016

3 Biotech

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A novel laccase-producing white-rot fungus, Marasmius sp. BBKAV79 (Genbank Accession Number-KP455496, KP455497), was isolated and subjected to purification, characterization and dye decolorization study. The purified enzyme was obtained with a specific activity of 0.226 U mg -1 protein and a final yield of 13.5 %. The enzyme was found to be a monomeric protein with a molecular mass of *75 kDa as estimated by non-denaturing polyacrylamide gel electrophoresis (PAGE) and further confirmed with zymogram analysis. The optimal pH and temperature of the laccase was recorded to be 5.5 and 40°C, respectively. The metal ions Hg 2? and Ag ? were found to drastically inhibit the activity of laccase at the rate of 96.6 and 96.5 %, respectively. Nevertheless, Fe 3? was found to inhibit laccase activity at 40 %. Phenylmethanesulfonyl fluoride (PMSF) strongly inhibited the laccase activity, and additives viz, sodium dodecyl sulfate (SDS), hydrogen peroxide (H 2 O 2 ) and sodium chloride (NaCl) were known to follow the earlier pattern of enzyme inhibition. The values of kinetic parameters K m and V max for purified laccase were noted at 3.03 mM and 5 lmol min -1 , respectively, for guaiacol as substrate. The textile dyes were decolorized at a range of 72-76 % and 88-93 % when treated with Marasmius sp. BBKAV79 and purified laccase, respectively. Based on the outcome of the present investigation, it could be, therefore, inferred that laccase isolated from Marasmius sp. BBKAV79 effectively decolorizes the textile dyes; however, the metal ions Hg 2? , Ag ? and Fe 3? and agents like PMSF, SDS, H 2 O 2 and NaCl pose an effective inhibitory potential under specified physicochemical conditions.

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Section: Resultssupporting

confidence: 55%

Purification and characterization of laccase from Marasmius species BBKAV79 and effective decolorization of selected textile dyes

Vantamuri

Kaliwal

2016

3 Biotech

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“…Enzymatic activities were assessed every 48 h from culture supernatants. Laccase extracellular activity was determined spectrophotometrically by the oxidation of ABTS (Nagai et al 2002). Cationic radical formation was detected by measuring the increase in absorbance at 420 nm (e420=36,000 M −1 cm −1 ).…”

Section: Enzymatic Assaysmentioning

confidence: 99%

Degradation of polycyclic aromatic hydrocarbons in soil by a tolerant strain of Trichoderma asperellum

Zafra

Moreno-Montaño

Absalón

et al. 2014

Environ Sci Pollut Res

100

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Trichoderma asperellum H15, a previously isolated strain characterized by its high tolerance to low (LMW) and high molecular weight (HMW) PAHs, was tested for its ability to degrade 3-5 ring PAHs (phenanthrene, pyrene, and benzo[a]pyrene) in soil microcosms along with a biostimulation treatment with sugarcane bagasse. T. asperellum H15 rapidly adapted to PAH-contaminated soils, producing more CO2 than uncontaminated microcosms and achieving up to 78 % of phenanthrene degradation in soils contaminated with 1,000 mg Kg(-1) after 14 days. In soils contaminated with 1,000 mg Kg(-1) of a three-PAH mixture, strain H15 was shown to degrade 74 % phenanthrene, 63 % pyrene, and 81 % of benzo[a]pyrene. Fungal catechol 1,2 dioxygenase, laccase, and peroxidase enzyme activities were found to be involved in the degradation of PAHs by T. asperellum. The results demonstrated the potential of T. asperellum H15 to be used in a bioremediation process. This is the first report describing the involvement of T. asperellum in LMW and HMW-PAH degradation in soils. These findings, along with the ability to remove large amounts of PAHs in soil found in the present work provide enough evidence to consider T. asperellum as a promising and efficient PAH-degrading microorganism.

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“…Therefore, further studies are needed to explain the reason why the laccase activity increases during storage under the alkaline condition. Compared with the laccase from fungi such as Myrothecium verrucaria NF-05 and Lentinula edodes, the recombinant CotA laccase was more stable over a wider pH range, especially under alkaline conditions (Nagai et al 2002;Zhao et al 2012). The pH optimum of B. subtilis CotA for ABTS, SGZ, and 2, 6-DMP oxidation was similar to the pH optimum of the B. licheniformis and B. pumilus Cot A laccases (Guan et al 2014;Koschorreck et al 2008;Lu et al 2013;Reiss et al 2011).…”

Section: Discussionmentioning

confidence: 78%

Expression of CotA laccase in Pichia pastoris and its electrocatalytic sensing application for hydrogen peroxide

Fan

Zhao

Wang

2015

Appl Microbiol Biotechnol

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The CotA laccase from Bacillus subtilis WD23 was successfully overexpressed in Pichia pastoris, and the production level reached 891.2 U/L. The recombinant CotA laccase was purified to homogeneity. The optimal enzymatic activity was found at pH 4.6, 6.6, and 6.8 for 2, 2'-azino-bis (3-ethylbenzothiazoline-6-sulfonate) (ABTS), 4-hydroxy-3, 5-dimethoxybenzaldehyde azine (SGZ), and 2, 6-dimethoxyphenol (2, 6-DMP) oxidation, respectively. The maximal enzyme activity was observed at 80 °C with SGZ as a substrate. The kinetic constant K m values for ABTS, SGZ, and 2, 6-DMP were 162 ± 20, 24 ± 2, and 166 ± 18 μM, respectively, with corresponding k cat values of 15 ± 1.0, 7.6 ± 1.5, and 0.87 ± 0.1 s(-1). Remarkably, the laccase activity increased to 561.9 % of its initial activity at pH 9.0 after 7 days of incubation and the half-life of laccase inactivation was approximately 3 h at 80 °C, which indicated that the recombinant CotA was a highly thermo-alkali-stable laccase. Bioelectrocatalytic reduction of H2O2 by the CotA laccase was detected when the recombinant CotA was adsorbed on pyrogenation graphite electrodes. Based on the bioelectrocatalytic reduction, a mediator-free amperometric biosensor for hydrogen peroxide was designed. The linear range of the H2O2 biosensor was from 0.05 to 4.75 mM, with a detection limit of 3.1 μM. The amperometric biosensor for H2O2 by CotA-modified electrode is a novel application for CotA laccase.

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Purification and characterization of an extracellular laccase from the edible mushroom Lentinula edodes , and decolorization of chemically different dyes

Cited by 232 publications

References 36 publications

Purification and characterization of laccase from Marasmius species BBKAV79 and effective decolorization of selected textile dyes

Purification and characterization of laccase from Marasmius species BBKAV79 and effective decolorization of selected textile dyes

Degradation of polycyclic aromatic hydrocarbons in soil by a tolerant strain of Trichoderma asperellum

Expression of CotA laccase in Pichia pastoris and its electrocatalytic sensing application for hydrogen peroxide

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