5 results match your criteria coccineus sanguineus

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Conserved white-rot enzymatic mechanism for wood decay in the Basidiomycota genus Pycnoporus.

DNA Res 2020 Apr;27(2)

INRAE, UMR1163, Biodiversity and Biotechnology of Fungi, Aix Marseille University, 13009 Marseille, France.

White-rot (WR) fungi are pivotal decomposers of dead organic matter in forest ecosystems and typically use a large array of hydrolytic and oxidative enzymes to deconstruct lignocellulose. However, the extent of lignin and cellulose degradation may vary between species and wood type. Here, we combined comparative genomics, transcriptomics and secretome proteomics to identify conserved enzymatic signatures at the onset of wood-decaying activity within the Basidiomycota genus Pycnoporus. Read More

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Visual Comparative Omics of Fungi for Plant Biomass Deconstruction.

Front Microbiol 2016 24;7:1335. Epub 2016 Aug 24.

Aix-Marseille Université, INRA, UMR1163, Biodiversité et Biotechnologie Fongiques Marseille, France.

Wood-decay fungi contain the cellular mechanisms to decompose such plant cell wall components as cellulose, hemicellulose, and lignin. A multi-omics approach to the comparative analysis of wood-decay fungi gives not only new insights into their strategies for decomposing recalcitrant plant biomass, but also an understanding of how to exploit these mechanisms for biotechnological applications. We have developed an analytical workflow, Applied Biomass Conversion Design for Efficient Fungal Green Technology (ABCDEFGT), to simplify the analysis and interpretation of transcriptomic and secretomic data. Read More

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September 2016

Phylogeographic relationships in the polypore fungus Pycnoporus inferred from molecular data.

FEMS Microbiol Lett 2011 Dec 3;325(1):37-48. Epub 2011 Oct 3.

INRA, UMR 1163 de Biotechnologie des Champignons Filamenteux, ESIL, Marseille, France.

The genus Pycnoporus forms a group of four species known especially for producing high redox potential laccases suitable for white biotechnology. A sample of 36 Pycnoporus strains originating from different geographical areas was studied to seek informative molecular markers for the typing of new strains in laboratory culture conditions and to analyse the phylogeographic relationships in this cosmopolitan group. ITS1-5. Read More

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December 2011

Pycnoporus laccase-mediated bioconversion of rutin to oligomers suitable for biotechnology applications.

Appl Microbiol Biotechnol 2011 Apr 6;90(1):97-105. Epub 2011 Jan 6.

UMR 1163 INRA de Biotechnologie des Champignons Filamenteux, ESIL, Case 925, 163 Avenue de Luminy, 13288, Marseille Cedex 09, France.

The Pycnoporus fungi are white-rot basidiomycetes listed as food- and cosmetic-grade microorganisms. Three high redox potential laccases from Pycnoporus coccineus and Pycnoporus sanguineus were tested and compared, with the commercial Suberase® as reference, for their ability to synthesise natural active oligomers from rutin (quercetin-3-rutinoside, one of the best-known naturally occurring flavonoid glycosides). The aim of this work was to develop a process with technical parameters (solvent, temperature, reaction time and raw materials) that were easy to scale up for industrial production and compatible with cosmetic and pharmaceutical formulation guidelines. Read More

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High redox potential laccases from the ligninolytic fungi Pycnoporus coccineus and Pycnoporus sanguineus suitable for white biotechnology: from gene cloning to enzyme characterization and applications.

J Appl Microbiol 2010 Jun 14;108(6):2199-213. Epub 2009 Nov 14.

UMR 1163 Biotechnologie des Champignons Filamenteux INRA-Universités de Provence et de la Méditerranée, ESIL, Case 925, Marseille Cedex, France.

Aims: Exploitation of natural biodiversity in species Pycnoporus coccineus and Pycnoporus sanguineus to screen for a new generation of laccases with properties suitable for the lignin-processing sector.

Methods And Results: Thirty strains originating from subtropical and tropical environments, mainly isolated from fresh specimens collected in situ, were screened for laccase activity. On the basis of levels of enzyme activity and percentage of similarity between protein sequences, the laccases from strains BRFM 938, BRFM 66 and BRFM 902 were selected for purification and characterization. Read More

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