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Decay resistance of anhydride-modified Corsican pine sapwood exposed to the brown rot fungus Coniophora puteana [PDF]

open access: yesHolzforschung, 2006
Abstract Corsican pine (Pinus nigra) sapwood was chemically modified with acetic or hexanoic anhydride to a variety of weight gains. The modified wood was exposed to the brown rot fungus Coniophora puteana, and the relationship between weight loss due to decay and weight percentage gain, or degree of hydroxyl substitution, was determined in
Graham Alan Ormondroyd
exaly   +4 more sources
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Mycelial interactions and outcrossing in the Coniophora puteana complex

Mycological Research, 1990
Outcrossing populations of the Coniophora puteana complex had a multiallelic unifactorial (bipolar) homogenic incompatibility (mating) system regulating the emergence of a secondary mycelium (stable mating-type heterokaryon) between paired single basidiospore-derived strains (homokaryons).
A.M. Ainsworth, A.D.M. Rayner
openaire   +1 more source

Characterization of the cellulolytic enzyme system from the brown-rot fungus Coniophora puteana

Applied Microbiology and Biotechnology, 1992
The cellulolytic enzymes of various strains of the brown-rot fungus Coniophora puteana were studied. The organism was grown in an air-lift fermentor in mineral medium containing glucose, cellobiose or amorphous cellulose. The specific growth rate varied between 0.082 and 0.062 h−1.
DiegoR. Schmidhalter   +1 more
openaire   +3 more sources

The biological effectiveness of wood modified with linear chain carboxylic acid anhydrides against Coniophora puteana

European Journal of Wood and Wood Products, 2002
Schneid) sapwood. A brown rot fungus [Coniophora puteana (Schum.:Fr)] was selected in order to determine and compare the effectiveness (threshold value) of the linear chain anhydrides. The work described in this paper has demonstrated that chemically modified Corsican pine sapwood afforded substantial bioprotection against Coniophora puteana.
Antonios N Papadopoulos
exaly   +2 more sources

Hybridization among cryptic species of the cellar fungus Coniophora puteana (Basidiomycota)

Molecular Ecology, 2007
AbstractIn this study we have analysed the genetic variation and phylogeography in a global sample of the cellar fungus Coniophora puteana, which is an important destroyer of wooden materials indoor. Multilocus genealogies of three DNA regions (beta tubulin, nrDNA ITS and translation elongation factor 1α) revealed the occurrence of three cryptic ...
Håvard, Kauserud   +3 more
openaire   +2 more sources

Characterization and Molecular Cloning of Cellobiose Dehydrogenase from the Brown-Rot Fungus Coniophora puteana

Journal of Bioscience and Bioengineering, 2004
Cellobiose dehydrogenase (CDH) was purified from the brown-rot fungus Coniophora puteana grown in culture containing crystalline cellulose as a carbon source. The purified enzyme gave a single band at 115 kDa on SDS-PAGE and showed a typical flavocytochrome absorption spectrum.
Taira, Kajisa   +5 more
openaire   +2 more sources

Growth of Coniophora puteana modified by a gall-inducing mycoparasite

Mycological Research, 1994
A gall-inducing mycoparasite, Nodulisporium cecidiogenes, which was found growing in association with living Coniophora puteana is described. In the presence of N. cecidiogenes, mycelial growth of C. puteana was reduced and colony colour and aerial mycelium were modified.
exaly   +2 more sources

Biodegradation of PAHs by Ligninolytic FungiHypoxylon FragiformeandConiophora Puteana

Polycyclic Aromatic Compounds, 2017
White-rot and brown-rot fungi degrade structural components of wood. The possibility of PAHs degradation by these fungi is based on their structural similarity with lignin (primary degraded by whit...
Mustafa Memić   +4 more
openaire   +1 more source

Improving the catalytic activity of β-glucosidase from Coniophora puteana via semi-rational design for efficient biomass cellulose degradation

Enzyme and Microbial Technology, 2023
In order to improve the degradation activity of β-glucosidase (CpBgl) from Coniophora puteana, the structural modification was conducted. The enzyme activity of mutants CpBgl-Q20C and CpBgl-A240S was increased by 65.75% and 58.58%, respectively. These mutants exhibited maximum activity under the same conditions as wild-type CpBgl (65 ℃ and pH 5.0 ...
Hai-Yan, Zhou   +11 more
openaire   +2 more sources

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