Purification and biochemical characterization of a laccase from the aquatic fungus Myrioconium sp. UHH 1-13-18-4 and molecular analysis of the laccase-encoding gene

Martín, Claudia Fernández; Pecyna, Marek J.; Kellner, Harald; Jehmlich, Nico; Junghanns, Charles; Benndorf, Dirk; Bergen, Martin von; Schlößer, Dietmar

doi:10.1007/s00253-007-1207-2

Cited by 17 publications

(6 citation statements)

References 55 publications

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“…In two varieties of G. gramminis, the gene sequences of LAC1 and LAC2 present 2 introns [33], just as in the single gene for extracellular laccase reported for the aquatic species Myrioconium sp. [34]. The presence of 3 introns has been reported in the lac2 gene [35] in the case of P. anserina and in the Bclcc1 and Bclcc2 genes of B. cinerea [4].…”

Section: Resultsmentioning

confidence: 94%

Structural and Phylogenetic Analysis of Laccases from Trichoderma: A Bioinformatic Approach

2013

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The genus Trichoderma includes species of great biotechnological value, both for their mycoparasitic activities and for their ability to produce extracellular hydrolytic enzymes. Although activity of extracellular laccase has previously been reported in Trichoderma spp., the possible number of isoenzymes is still unknown, as are the structural and functional characteristics of both the genes and the putative proteins. In this study, the system of laccases sensu stricto in the Trichoderma species, the genomes of which are publicly available, were analyzed using bioinformatic tools. The intron/exon structure of the genes and the identification of specific motifs in the sequence of amino acids of the proteins generated in silico allow for clear differentiation between extracellular and intracellular enzymes. Phylogenetic analysis suggests that the common ancestor of the genus possessed a functional gene for each one of these enzymes, which is a characteristic preserved in T. atroviride and T. virens. This analysis also reveals that T. harzianum and T. reesei only retained the intracellular activity, whereas T. asperellum added an extracellular isoenzyme acquired through horizontal gene transfer during the mycoparasitic process. The evolutionary analysis shows that in general, extracellular laccases are subjected to purifying selection, and intracellular laccases show neutral evolution. The data provided by the present study will enable the generation of experimental approximations to better understand the physiological role of laccases in the genus Trichoderma and to increase their biotechnological potential.

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Section: Resultsmentioning

confidence: 94%

Structural and Phylogenetic Analysis of Laccases from Trichoderma: A Bioinformatic Approach

2013

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“…In contrast the affinity ( K m value) of the Myrioconium sp. laccase towards typical laccase substrates follows the rank order syringaldazine > DMP > ABTS, where DMP is more specific substrate than ABTS for laccase (Martin et al 2007). The values reported for the parameter, K cat , is a representation of the rate the catalytic process (Table 2).…”

Section: Resultsmentioning

confidence: 99%

Purification and characterization of an extracellular laccase from solid-state culture of Pleurotus ostreatus HP-1

Patel¹,

Gupte²,

Gahlout³

et al. 2013

3 Biotech

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A native isolate of Pleurotus ostreatus HP-1 (Genbank Accession No. EU420068) was found to have an excellent laccase producing ability. The extracellular laccase was purified to electrophoretic homogeneity from copper sulphate induced solid-state fermentation medium by ammonium sulphate precipitation and ion-exchange chromatography. The enzyme was determined to be monomeric protein with an apparent molecular mass of 68,420 kDa, and an isoelectric point (pI) of 3.5. The inductively coupled plasma spectroscopy showed a presence of iron, zinc and copper in the purified enzyme. The absorption spectrum in the range of 200–700 nm showed the maximum absorption at 610 nm characteristic of fungal laccase and corresponding to the presence of type I copper atom. The laccase was stable at different temperatures up to 70 °C and retained 61 % activity at 50 °C. The enzyme reaction was inhibited by cysteine; sodium azide and EDTA. The enzyme oxidized various known laccase substrates, its lowest Km value being for ortho-dianisidine and highest Kcat and Kcat/Km for ABTS. The purified laccase exhibited different pH optima for different substrates. The N-terminal sequence did not show any similarity with N-terminal sequence of other species of genera Pleurotus.

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“…UHH 1-13-18 [68], and in the ascomycete Hortea acidophila [69] implying their potential role in copper induction of laccase expression.…”

Section: Laccase Promoters Sequence Analysismentioning

confidence: 99%

Induction and Transcriptional Regulation of Laccases in Fungi

Piscitelli

Giardina²,

Lettera³

et al. 2011

285

219

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Fungal laccases are phenol oxidases widely studied for their use in several industrial applications, including pulp bleaching in paper industry, dye decolourisation, detoxification of environmental pollutants and revalorization of wastes and wastewaters. The main difficulty in using these enzymes at industrial scale ensues from their production costs. Elucidation of the components and the mechanisms involved in regulation of laccase gene expression is crucial for increasing the productivity of native laccases in fungi. Laccase gene transcription is regulated by metal ions, various aromatic compounds related to lignin or lignin derivatives, nitrogen and carbon sources. In this manuscript, most of the published results on fungal laccase induction, as well as analyses of both the sequences and putative functions of laccase gene promoters are reviewed. Analyses of promoter sequences allow defining a correlation between the observed regulatory effects on laccase gene transcription and the presence of specific responsive elements, and postulating, in some cases, a mechanism for their functioning. Only few reports have investigated the molecular mechanisms underlying laccase regulation by different stimuli. The reported analyses suggest the existence of a complex picture of laccase regulation phenomena acting through a variety of cis acting elements. However, the general mechanisms for laccase transcriptional regulation are far from being unravelled yet.

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Purification and biochemical characterization of a laccase from the aquatic fungus Myrioconium sp. UHH 1-13-18-4 and molecular analysis of the laccase-encoding gene

Cited by 17 publications

References 55 publications

Structural and Phylogenetic Analysis of Laccases from Trichoderma: A Bioinformatic Approach

Structural and Phylogenetic Analysis of Laccases from Trichoderma: A Bioinformatic Approach

Purification and characterization of an extracellular laccase from solid-state culture of Pleurotus ostreatus HP-1

Induction and Transcriptional Regulation of Laccases in Fungi

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