Diversity of bacterial laccase-like multicopper oxidase genes in forest and grassland Cambisol soil samples

Kellner, Harald; Luis, Patricia; Zimdars, Bettina; Kiesel, Bärbel; Buscot, François

doi:10.1016/j.soilbio.2007.09.013

Cited by 100 publications

(67 citation statements)

References 34 publications

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“…LMCO nucleotide sequences from this study did not cluster with previously studied ones from forest [23] and peat soil [29]. However, sequences clustered with LMCO sequences (LN559552 and HE613083) retrieved from agricultural compost that shows similarity with activated sludge of pulp and paper industry in the type of organic matter or partially degraded organic matter which proposed that LMCOs with same functions may have similar sequences.…”

Section: Laccase Diversitycontrasting

confidence: 64%

“…The PCR reaction was performed on the extracted DNA samples using degenerate primers Cu1AF (ACMWCBG-TYCAYTGGCAYGG) and Cu2R (GRCTGTGGTACCA-GAANGTNCC) [23] for the amplification of conserved LMCO gene region. Each PCR reaction contained 1X Taq buffer, 2 mM MgCl 2 , 1.5 U Taq Polymerase (Fermentas), 200 lM dNTP's, 1.2 lM of each primer, 50 ng extracted DNA and nuclease free water in the final reaction volume of 20 ll.…”

Section: Amplification Cloning and Sequencing Of Lmco Genesmentioning

confidence: 99%

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Bio-Prospecting Laccases in the Bacterial Diversity of Activated Sludge From Pulp and Paper Industry

et al. 2016

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Activated sludge is an artificial ecosystem known to harbor complex microbial communities. Bacterial diversity in activated sludge from pulp and paper industry was studied to bioprospect for laccase, the multicopper oxidase applicable in a large number of industries due to its ability to utilize a wide range of substrates. Bacterial diversity using 454 pyrosequencing and laccase diversity using degenerate primers specific to conserved copper binding domain of laccase like multicopper oxidase (LMCO) genes were investigated. 1231 OTUs out of 11,425 sequence reads for bacterial diversity and 11 OTUs out of 15 reads for LMCO diversity were formed. Phylum Proteobacteria (64.95 %) with genus Thauera (13.65 %) was most abundant followed by phylum Bacteriodetes (11.46 %) that included the dominant genera Paludibacter (1.93 %) and Lacibacter (1.32 %). In case of LMCOs, 40 % sequences showed affiliation with Proteobacteria and 46.6 % with unculturable bacteria, indicating considerable novelty, and 13.3 % with Bacteroidetes. LMCOs belonged to H and J families.

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Section: Laccase Diversitycontrasting

confidence: 64%

Section: Amplification Cloning and Sequencing Of Lmco Genesmentioning

confidence: 99%

Bio-Prospecting Laccases in the Bacterial Diversity of Activated Sludge From Pulp and Paper Industry

et al. 2016

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“…Therefore, metagenomic analyses facilitate the discovery of novel genes in biological communities by overcoming the limitations of cultivation-dependent approaches (Guazzaroni et al 2015;Leis et al 2013). Kellner et al analyzed the diversity of bacterial laccase genes in samples from forests and grasslands and found 16 distinct sequence-type clades of bacterial laccase (Kellner et al 2008). Kellenberger et al evaluated the spatial distribution and function of fungal laccase genes from a forest cambisol (Kellenberger 2001).…”

Section: Open Accessmentioning

confidence: 99%

Identification of bacterial laccase cueO mutation from the metagenome of chemical plant sludge

Yue

Yang

Zhao

et al. 2017

Bioresour. Bioprocess.

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Background:The metagenome contains plenty of genetic resources and can be used to search for the novel gene or mutant. Results:In this study, the bacterial laccase gene (cueO) with single or multiple mutations was directly cloned based on the metagenome of a chemical plant sludge. An interesting mutation (G276R) was identified from those cloned mutants. The other mutants (G276N, G276Y, and G276K) with improved catalytic efficiency were identified by the saturation mutagenesis on residue G276. The optimal temperature for wild-type CueO enzyme activity was about 70 °C, compared to 60 °C, 50 °C, 50 °C, and 30 °C for the G276R, G276N, G276Y, and G276K mutant enzymes, respectively. The catalytic efficiency (k cat /K m ) with 8 mmol Cu 2+ of the G276R, G276N, G276Y, and G276K mutants was 1.2-, 2.7-, 1.3-, and 2.7-fold, respectively, compared to the wild-type enzyme. In addition, the mutants G276R, G276N, G276Y, and G276K oxidized the carcinogen benzo[α]pyrene more efficiently compared to the wild-type enzyme. Conclusion:All of the results indicate that G276 of CueO plays an important role in enzyme activity, and the useful mutants can be identified based on the metagenome.

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“…DyP-type peroxidases are less complex than the other heme peroxidases and are common among bacteria [11,44], including the extracellular enzyme systems of Thermobifida fusca and Rhodococcus jostii [69,77]. Several bacterial laccases have also been identified [78][79][80] including multiple laccase-like multi-copper oxidases in Agromyces salentinus and Sinorhizobium morelense [78]. Even if the knowledge concerning bacterial peroxidases and laccases has grown recently, additional-as yet undiscovered-enzymes may be required for bacterial lignin degradation, for example, oxidases for the production of H 2 O 2 .…”

Section: Bacterial Lignin Degradationmentioning

confidence: 99%

Lignin Degradation Processes and the Purification of Valuable Products

Schoenherr¹,

Ebrahimi²,

Czermak³

2018

Lignin - Trends and Applications

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Lignin is a heterogeneous, phenolic and polydisperse biopolymer which resists degradation due to its aromatic and highly branched structure. Lignin is the most abundant renewable source of aromatic molecules on earth. The valorization of lignin could therefore provide a sustainable alternative to petroleum refineries for the production of valuable aromatic compounds. Even so, paper mills and lignocellulose feedstock biorefineries treat lignin largely as a waste product. In paper mills, 98% of technical lignin is incinerated for internal energy recovery while only 2% is used commercially (e.g. for the production of aromatics such as vanillin). The reasons for the underutilization of lignin include its recalcitrance to degradation and the challenge of separating mixtures of numerous degradation products. The successful valorization of lignin in the future thus depends on a broad understanding of biological and technical degradation processes, and the implementation of efficient product purification strategies. This article describes enzymatic, photocatalytic and thermochemical lignin degradation processes and considers purification methods for valuable lignin-derived degradation products. We focus on the potential of membrane-based separation technology, including data from our own recent research.

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Diversity of bacterial laccase-like multicopper oxidase genes in forest and grassland Cambisol soil samples

Cited by 100 publications

References 34 publications

Bio-Prospecting Laccases in the Bacterial Diversity of Activated Sludge From Pulp and Paper Industry

Bio-Prospecting Laccases in the Bacterial Diversity of Activated Sludge From Pulp and Paper Industry

Identification of bacterial laccase cueO mutation from the metagenome of chemical plant sludge

Lignin Degradation Processes and the Purification of Valuable Products

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