Degradation and Transformation of Aquatic Humic Substances by Laccase-producing FungiCladosporium cladosporioides andPolyporus versicolor

Claus, H.; Filip, Z.

doi:10.1002/(sici)1521-401x(199805)26:3<180::aid-aheh180>3.0.co;2-9

Cited by 46 publications

(22 citation statements)

References 28 publications

(47 reference statements)

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“…ABTS oxidation by Myrothecium verrucaria and probably also by Acremonium murorum was probably due to bilirubin oxidase, another Cucontaining oxidase (Baldrian 2006;Hoegger et al 2006). Cladosporium cladosporoides and a Penicillium strain were also previously reported to degrade lignin-like compounds (Claus and Filip 1998;Zheng et al 1999) or humic acids (Gramss et al 1999;Paul and Mathur 1967), however, the identity of the enzymes involved remains unclear.…”

Section: Discussionmentioning

confidence: 99%

Production of extracellular enzymes and degradation of biopolymers by saprotrophic microfungi from the upper layers of forest soil

et al. 2010

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Production of extracellular enzymes participating in the degradation of biopolymers was studied in 29 strains of nonbasidiomycetous microfungi isolated from Quercus petraea forest soil based on the frequency of occurrence. Most of the isolates were ascomycetes and belonged to the genera Acremonium, Alternaria, Cladosporium, Geomyces, Hypocrea, Myrothecium, Ochrocladosporium, and Penicillium (18 isolates), and two isolates were zygomycetes. Only six isolates showed phenol oxidation activity which was low and none of the strains were able to degrade humic acids. Approximately half of the strains were able to degrade cellulose and all but six degraded chitin. Most strains produced significant amounts of the cellulolytic enzymes cellobiohydrolase and β-glucosidase and the chitinolytic enzymes chitinase, chitobiosidase, and N-acetylglucosaminidase. The highest cellulase activities were found in Penicillium strains, and the highest activity of chitinolytic enzymes was found in Acremonium sp. The production of the hemicellulose-degrading enzymes α-galactosidase, β-galactosidase, and α-mannosidase was mostly low.The microfungal strains were able to produce significant growth on a range of 41-87, out of 95 simple Ccontaining substrates tested in a Biolog™ assay, monosaccharides being for all strains the most rapidly metabolized C-sources. Comparison with saprotrophic basidiomycetes from the same environment showed that microfungi have similar cellulolytic capabilities and higher chitinase activities which testifies for their active role in the decomposition of both lignocellulose and dead fungal biomass, important pools of soil carbon.

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Section: Discussionmentioning

confidence: 99%

Production of extracellular enzymes and degradation of biopolymers by saprotrophic microfungi from the upper layers of forest soil

et al. 2010

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“…2. Degradation of polymers: Laccases are involved in the degradation of complex natural polymers, such as lignin Eriksson 1994, Thurston 1994) or humic acids (Claus and Filip 1998). The reactive radicals generated lead to the cleavage of covalent bonds (especially alkyl-aryl-) and to the release of monomers.…”

Section: Substrates and Reaction Mechanismsmentioning

confidence: 99%

Laccases and their occurrence in prokaryotes

2003

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Laccases are copper-containing proteins that require O(2) to oxidize phenols, polyphenols, aromatic amines, and different non-phenolic substrates by one-electron transfer, resulting in the formation of reactive radicals. Although their specific physiological functions are not completely understood, there are several indications that laccases are involved in the morphogenesis of microorganisms (e.g., fungal spore development, melanization) and in the formation and/or degradation of complex organic substances such as lignin or humic matter. Owing to their high relative non-specific oxidation capacity, laccases are useful biocatalysts for diverse biotechnological applications. To date, laccases have been found only in eukaryotes (fungi, plants); however, databank searches and experimental data now provide evidence for their distribution in prokaryotes. This survey shows that laccase-like enzymes occur in many gram-negative and gram-positive bacteria. Corresponding genes have been found in prokaryotes that are thought to have branched off early during evolution, e.g., the extremely thermophilic Aquifex aeolicus and the archaeon Pyrobaculum aerophilum. Phylogenetically, the enzymes are members of the multi-copper protein family that have developed from small-sized prokaryotic azurins to eukaryotic plasma proteins.

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“…From the above results it is clear that the maximum decolorization of acid blue 193 is mainly due to the presence of laccase enzyme. However Claus & Filip (1998) reported the formation of laccase with low decolorizing activity during the transformation of aquatic humic substances by Cladosporium cladosporioides.…”

Section: Growth Behavior Of Cladosporium Cladosporioides With Decolormentioning

confidence: 99%

Decolorization of 1:2 metal complex dye Acid blue 193 by a newly isolated fungus, Cladosporium cladosporioides

Vijaykumar

Veeranagouda

Neelakanteshwar

et al. 2005

World J Microbiol Biotechnol

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Degradation and Transformation of Aquatic Humic Substances by Laccase-producing FungiCladosporium cladosporioides andPolyporus versicolor

Cited by 46 publications

References 28 publications

Production of extracellular enzymes and degradation of biopolymers by saprotrophic microfungi from the upper layers of forest soil

Production of extracellular enzymes and degradation of biopolymers by saprotrophic microfungi from the upper layers of forest soil

Laccases and their occurrence in prokaryotes

Decolorization of 1:2 metal complex dye Acid blue 193 by a newly isolated fungus, Cladosporium cladosporioides

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