Irpex lacteus , a white rot fungus applicable to water and soil bioremediation

Novotný, Čeněk; Erbanová, Pavla; Cajthaml, Tomáš; Rothschild, Nathan; Dosoretz, Carlos G.; Šašek, V.

doi:10.1007/s002530000432

Cited by 116 publications

(43 citation statements)

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“…However, with Euc-1 the same features were not observed. In the case of I. lacteus, laccase activity was not detected though in other studies the presence of low activity of this enzyme in the presence of other carbon sources has been determined (Novotny et al, 2000). These differences could be interpreted as the result of different incubation periods and/or by the presence of different growth media composition (Dinis et al, 2009).…”

Section: Ligninolytic Potential Of Fungal Isolatesmentioning

confidence: 91%

Enzymatic saccharification of biologically pre-treated wheat straw with white-rot fungi

Dias

Freitas

Marques

et al. 2010

Bioresource Technology

147

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a b s t r a c tWheat straw was submitted to a pre-treatment by the basidiomycetous fungi Euc-1 and Irpex lacteus, aiming to improve the accessibility of cellulose towards enzymatic hydrolysis via previous selective bio-delignification. This allowed the increase of substrate saccharification nearly four and three times while applying the basidiomycetes Euc-1 and I. lacteus, respectively. The cellulose/lignin ratio increased from 2.7 in the untreated wheat straw to 5.9 and 4.6 after the bio-treatment by the basidiomycetes Euc-1 and I. lacteus, respectively, thus evidencing the highly selective lignin biodegradation. The enzymatic profile of both fungi upon bio-treatment of wheat straw have been assessed including laccase, manganese-dependent peroxidase, lignin peroxidase, carboxymethylcellulase, xylanase, avicelase and feruloyl esterase activities. The difference in efficiency and selectivity of delignification within the two fungi treatments was interpreted in terms of specific lignolytic enzyme profiles and moderate xylanase and cellulolytic activities.

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Section: Ligninolytic Potential Of Fungal Isolatesmentioning

confidence: 91%

Enzymatic saccharification of biologically pre-treated wheat straw with white-rot fungi

Dias

Freitas

Marques

et al. 2010

Bioresource Technology

147

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“…(Xu, 1996). Consequently, laccases have evoked particular interest in biotechnological applications, ranging from biopulping (Wong et al, 2000) to remediation of wastewater (Novotny et al, 2000) containing recalcitrant contaminants (D'Annibale et al, 1998) Several plant and fungal laccases are known, having been isolated and characterized spectroscopically and biochemically. Several other laccases are known based on the protein or cDNA sequence information.…”

Section: Introductionmentioning

confidence: 99%

Combined sequence and structure analysis of the fungal laccase family

Kumar

Phale

Durani

et al. 2003

Biotech & Bioengineering

192

152

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Plant and fungal laccases belong to the family of multi-copper oxidases and show much broader substrate specificity than other members of the family. Laccases have consequently been of interest for potential industrial applications. We have analyzed the essential sequence features of fungal laccases based on multiple sequence alignments of more than 100 laccases. This has resulted in identification of a set of four ungapped sequence regions, L1-L4, as the overall signature sequences that can be used to identify the laccases, distinguishing them within the broader class of multi-copper oxidases. The 12 amino acid residues in the enzymes serving as the copper ligands are housed within these four identified conserved regions, of which L2 and L4 conform to the earlier reported copper signature sequences of multi-copper oxidases while L1 and L3 are distinctive to the laccases. The mapping of regions L1-L4 on to the three-dimensional structure of the Coprinus cinerius laccase indicates that many of the non-copper-ligating residues of the conserved regions could be critical in maintaining a specific, more or less C-2 symmetric, protein conformational motif characterizing the active site apparatus of the enzymes. The observed intraprotein homologies between L1 and L3 and between L2 and L4 at both the structure and the sequence levels suggest that the quasi C-2 symmetric active site conformational motif may have arisen from a structural duplication event that neither the sequence homology analysis nor the structure homology analysis alone would have unraveled. Although the sequence and structure homology is not detectable in the rest of the protein, the relative orientation of region L1 with L2 is similar to that of L3 with L4. The structure duplication of first-shell and second-shell residues has become cryptic because the intraprotein sequence homology noticeable for a given laccase becomes significant only after comparing the conservation pattern in several fungal laccases. The identified motifs, L1-L4, can be useful in searching the newly sequenced genomes for putative laccase enzymes.

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“…This white-rot fungus has been applied in biodegradation of toxic compounds (1), dye decolorization (2), water and soil bioremediation (3), and biopretreatment of lignocellulosic substrates to improve sugar recoveries for bioethanol production (4,5). Its efficiency in these processes has been mainly attributed to the release of a battery of ligninolytic enzymes, namely, Mn 2ϩ -oxidizing peroxidases (MnPs), lignin peroxidases (LiPs), and laccases (6).…”

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confidence: 99%

Characterization of a Novel Dye-Decolorizing Peroxidase (DyP)-Type Enzyme from Irpex lacteus and Its Application in Enzymatic Hydrolysis of Wheat Straw

Salvachúa

Prieto

Martı́nez

et al. 2013

Appl Environ Microbiol

135

122

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Irpex lacteus is a white rot basidiomycete proposed for a wide spectrum of biotechnological applications which presents an interesting, but still scarcely known, enzymatic oxidative system. Among these enzymes, the production, purification, and identification of a new dye-decolorizing peroxidase (DyP)-type enzyme, as well as its physico-chemical, spectroscopic, and catalytic properties, are described in the current work. According to its N-terminal sequence and peptide mass fingerprinting analyses, I. lacteus DyP showed high homology (>95%) with the hypothetical (not isolated or characterized) protein cpop21 from an unidentified species of the family Polyporaceae. The enzyme had a low optimal pH, was very stable to acid pH and temperature, and showed improved activity and stability at high H 2 O 2 concentrations compared to other peroxidases. Other attractive features of I. lacteus DyP were its high catalytic efficiency oxidizing the recalcitrant anthraquinone and azo dyes assayed (k cat /K m of 1.6 ؋ 10 6 s ؊1 M ؊1 ) and its ability to oxidize nonphenolic aromatic compounds like veratryl alcohol. In addition, the effect of this DyP during the enzymatic hydrolysis of wheat straw was checked. The results suggest that I. lacteus DyP displayed a synergistic action with cellulases during the hydrolysis of wheat straw, increasing significantly the fermentable glucose recoveries from this substrate. These data show a promising biotechnological potential for this enzyme.

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Irpex lacteus , a white rot fungus applicable to water and soil bioremediation

Cited by 116 publications

References 0 publications

Enzymatic saccharification of biologically pre-treated wheat straw with white-rot fungi

Enzymatic saccharification of biologically pre-treated wheat straw with white-rot fungi

Combined sequence and structure analysis of the fungal laccase family

Characterization of a Novel Dye-Decolorizing Peroxidase (DyP)-Type Enzyme from Irpex lacteus and Its Application in Enzymatic Hydrolysis of Wheat Straw

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