Effects of pollutants on laccase activities of Marasmius quercophilus, a white-rot fungus isolated from a Mediterranean schlerophyllous litter

Farnet, Anne‐Marie; Gil, G.; Ferre, E.

doi:10.1016/j.chemosphere.2007.06.086

Cited by 40 publications

(31 citation statements)

References 25 publications

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“…Heavy metal ions which are common environmental pollutants with strong toxicity can affect the activity and stability of laccase [37]. However, this enzyme was not affected by the addition of metal ions such as Cu 2+ , Mn 2+ , Zn 2+ , Na + , K + , Mg 2+ , Ba 2+ , and Ca 2+ at 5 mM, and it was slightly promoted by Cu 2+ , Mn 2+ , Zn 2+ , and Na + .…”

Section: Discussionmentioning

confidence: 96%

Production of a thermostable metal-tolerant laccase from Trametes versicolor and its application in dye decolorization

Zhang

Cao

et al. 2011

Biotechnol Bioproc E

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Production of laccase using a submerged culture of Trametes versicolor sdu-4 was optimized using a central composite design of the Response Surface Methodology. Optimized conditions gave a laccase yield of 4,213 U/L which was approximately three times of that in basal medium. The laccase was purified to homogeneity using a three-step process. The overall yield of the purification was 58%, with a purification fold of 11.4 and a specific activity of 1320.7 U/mg protein. The molecular mass of the laccase was 60 kDa. The optimum pH values of the enzyme were 2.2, 3.7, and 7 for the oxidations of ABTS, DMP, and syringaldazine, respectively. The enzyme had adaptability to a broad pH range and high temperature and wsa stable at pH 3.0 ~ 10.0. The half-life of this laccase at 70°C was 2.2 h. Methyl red, 2-bromophenol, and 4-bromophenol were oxidized by the purified laccase in the absence of mediators. Purified laccase was effective in the decolorization of several dyes and was not inhibited by Cu 2+ , Mn 2+ , Zn 2+ , Na + , K + , Mg 2+ , Ba 2+ , and Ca 2+ at 5 mM. These excellent characteristics made it a highly attractive candidate for industrial use.

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Section: Discussionmentioning

confidence: 96%

Production of a thermostable metal-tolerant laccase from Trametes versicolor and its application in dye decolorization

Zhang

Cao

et al. 2011

Biotechnol Bioproc E

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“…In contrast, CuSO 4 or MnSO 4 (10 mM) showed no inhibition to the enzyme activity. In comparison to the laccases from other white-rot fungi [28][29][30] including an isolate of Pycnoporus 31 , it was found that P. coccineus Thongkred 013 BCU laccase was more sensitive to SDS, EDTA, and almost all ions tested, except for Mn 2+ .…”

Section: Fungal Collection and Screening For Laccase Producermentioning

confidence: 90%

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Thongkred¹,

Lotrakul²,

Prasongsuk³

et al. 2011

ScienceAsia

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Basidiocarps of Pycnoporus coccineus and P. sanguineus were collected from Kanchanaburi, Phetchaburi, and Mae Hong Son provinces in Thailand. Liquid culture of P. coccineus isolates provided higher laccase and manganese peroxidase activities than those of P. sanguineus. Lignin peroxidase activity was not detectable in any of the three Pycnoporus isolates. P. coccineus Thongkred 013 BCU, the best laccase producer among these isolates, was selected to optimize laccase production. The highest laccase yield (5.97 ± 0.40 U/ml) was obtained when grown at 28°C for 8 days in basal medium containing 2% (w/v) glucose and 0.25% (w/v) peptone at an initial pH of 5.0. The optimum conditions for stability and activity of the crude laccase enzyme were at pH 3.5 and room temperature (25 ± 2°C). FeSO4 (10 mM) and SDS (1% w/v) were both inhibitory to the laccase activity. When five different types of polycyclic aromatic hydrocarbons (PAHs) were individually added to liquid culture of P. coccineus at 100 ppm, the oxidation of anthracene, pyrene, and fluoranthene detected within 24 h were 59.7, 50.7, and 49.8%, respectively, whereas only 25.3% of benzo[a]pyrene and 32.4% of phenanthrene were oxidized. When P. coccineus crude laccase (1 U/ml) was used, these PAHs were more readily oxidized, with 76.4 and 74.3% of pyrene and anthracene, respectively, being oxidized within 2 h and 84.2% of fluoranthene oxidized within 24 h. Benzo[a]pyrene and phenanthrene oxidation by the enzyme were enhanced when 1 mM 2,2'-azinobis(3-ethylbenzothiazoline-6-sulphonic acid) was added as a mediator to the reaction mixture, resulting in 66.3 and 50.5% of the initial 100 ppm being oxidized after 24 h.

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“…Laccase of Bacillus sp. HR03 lost half of its activity at 0.7 M of NaCl, while 7.5 mM of NaCl inhibited 50% of laccase activity from a white-rot fungus, Marasmius quercophilus [13]. Furthermore, the enzyme from Bacillus halodurans was stimulated rather than inhibited with increasing concentrations of NaCl (up to 100 mM) [27].…”

Section: Biochemical Characterization Of Cotamentioning

confidence: 98%

Enhanced expression of a recombinant bacterial laccase at low temperature and microaerobic conditions: purification and biochemical characterization

Mohammadian

Fathi‐Roudsari

Mollania

et al. 2010

J Ind Microbiol Biotechnol

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Laccases (benzenediol oxygen oxidoreductase; EC 1.10.3.2) have many biotechnological applications because of their oxidation ability towards a wide range of phenolic compounds. Within recent years, researchers have been highly interested in the identification and characterization of laccases from bacterial sources. In this study, we have isolated and cloned a gene encoding laccase (CotA) from Bacillus sp. HR03 and then expressed it under microaerobic conditions and decreased temperature in order to obtain high amounts of soluble protein. The laccase was purified and its biochemical properties were investigated using three common laccase substrates, 2,2'-azino-bis (3-ethylbenzothiazoline-6-sulphonic acid) (ABTS), syringaldazine (SGZ) and 2,6-dimethoxyphenol (2,6-DMP). K(M) and k(cat) were calculated 535 microM and 127 s(-1) for ABTS, 53 microM and 3 s(-1) for 2, 6-DMP and 5 microM and 20 s(-1) for SGZ when the whole reactions were carried out at room temperature. Laccase activity was also studied when the enzyme was preincubated at 70 and 80 degrees C. With SGZ as the substrate, the activity was increased three-fold after 50 min preincubation at 70 degrees C and 2.4-fold after 10 min preincubation at 80 degrees C. Preincubation of the enzyme in 70 degrees C for 30 min raised the activity four-fold with ABTS as the substrate. Also, L-dopa was used as a substrate. The enzyme was able to oxidize L-dopa with the K(M) and k(cat) of 1,493 microM and 194 s(-1), respectively.

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Effects of pollutants on laccase activities of Marasmius quercophilus, a white-rot fungus isolated from a Mediterranean schlerophyllous litter

Cited by 40 publications

References 25 publications

Production of a thermostable metal-tolerant laccase from Trametes versicolor and its application in dye decolorization

Production of a thermostable metal-tolerant laccase from Trametes versicolor and its application in dye decolorization

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Enhanced expression of a recombinant bacterial laccase at low temperature and microaerobic conditions: purification and biochemical characterization

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