Isolation and Characterization of the Cellobiose Dehydrogenase from the Brown-Rot Fungus Coniophora puteana (Schum ex Fr.) Karst.

Schmidhalter, Diego R.; Canevascini, Giorgio

doi:10.1006/abbi.1993.1077

Cited by 53 publications

(31 citation statements)

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“…The only characterized brown rot fungal CDH is from C. puteana. It oxidizes both cellobiose and cellooligosaccharides but not glucose, which supports the typical catalytic properties of CDH (120,121).…”

Section: Cellulose-degrading Enzymessupporting

confidence: 66%

Plant-Polysaccharide-Degrading Enzymes from Basidiomycetes

Rytioja

Hildén

Yuzon

et al. 2014

Microbiol Mol Biol Rev

348

287

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SUMMARY Basidiomycete fungi subsist on various types of plant material in diverse environments, from living and dead trees and forest litter to crops and grasses and to decaying plant matter in soils. Due to the variation in their natural carbon sources, basidiomycetes have highly varied plant-polysaccharide-degrading capabilities. This topic is not as well studied for basidiomycetes as for ascomycete fungi, which are the main sources of knowledge on fungal plant polysaccharide degradation. Research on plant-biomass-decaying fungi has focused on isolating enzymes for current and future applications, such as for the production of fuels, the food industry, and waste treatment. More recently, genomic studies of basidiomycete fungi have provided a profound view of the plant-biomass-degrading potential of wood-rotting, litter-decomposing, plant-pathogenic, and ectomycorrhizal (ECM) basidiomycetes. This review summarizes the current knowledge on plant polysaccharide depolymerization by basidiomycete species from diverse habitats. In addition, these data are compared to those for the most broadly studied ascomycete genus, Aspergillus , to provide insight into specific features of basidiomycetes with respect to plant polysaccharide degradation.

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Section: Cellulose-degrading Enzymessupporting

confidence: 66%

Plant-Polysaccharide-Degrading Enzymes from Basidiomycetes

Rytioja

Hildén

Yuzon

et al. 2014

Microbiol Mol Biol Rev

348

287

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“…CDH was first purified from C. puteana by Schmidhalter & Canevascini (1993). Postulated roles in other fungi include prevention of snap-back (i.e.…”

Section: Introductionmentioning

confidence: 99%

A Mechanism for Production of Hydroxyl Radicals by the Brown-Rot Fungus Coniophora Puteana: Fe(III) Reduction by Cellobiose Dehydrogenase and Fe(II) Oxidation at a Distance from the Hyphae

Hyde

Wood²

1997

Microbiology

187

125

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In timber infested by brown-rot fungi, a rapid loss of strength is attributed to production of hydroxyl radicals (HO.). The hydroxyl radicals are produced by the Fenton reaction [Fe(II)/H2O2], but the pathways leading to Fe(II) and H2O2 have remained unclear. Cellobiose dehydrogenase, purified from cultures of Coniophora puteana, has been shown to couple oxidation of cellodextrins to conversion of Fe(III) to Fe(II). Two characteristics of brown rot are release of oxalic acid and lowering of the local pH, often to about pH 2. Modelling of Fe(II) speciation in the presence of oxalate has revealed that Fe(II)-oxalate complexes are important at pH 4-5, but at pH 2 almost all Fe(II) is in an uncomplexed state which reacts very slowly with dioxygen. Diffusion of Fe(II) away from the hyphae will promote conversion to Fe(II)-oxalate and autoxidation with H2O2 as product. Thus the critical Fe(II)/H2O2 combination will be generated at a distance, enabling hydroxyl radicals to be formed without damage to the hyphae.

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“…Cellobiose dehydrogenase has been isolated and characterized from a variety of white-rot fungi (2,6,21,38,43,53), soft-rot fungi (13,15,20,50,52), and one brown-rot fungus (49). Typically, CDH is a monomeric protein consisting of two domains, one containing a hexacoordinate heme b (14) and one containing a noncovalently bound flavin adenine dinucleotide (FAD) (6,43) or 6-hydroxy FAD (33).…”

mentioning

confidence: 99%

Purification and Characterization of Cellobiose Dehydrogenase from the Plant PathogenSclerotium(Athelia)rolfsii

Baminger

Subramaniam

Renganathan

et al. 2001

Appl Environ Microbiol

121

108

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Cellobiose dehydrogenase (CDH) is an extracellular hemoflavoenzyme produced by several wood-degrading fungi. In the presence of a suitable electron acceptor, e.g., 2,6-dichloro-indophenol (DCIP), cytochrome c, or metal ions, CDH oxidizes cellobiose to cellobionolactone. The phytopathogenic fungus Sclerotium rolfsii (teleomorph: Athelia rolfsii) strain CBS 191.62 produces remarkably high levels of CDH activity when grown on a cellulose-containing medium. Of the 7,500 U of extracellular enzyme activity formed per liter, less than 10% can be attributed to the proteolytic product cellobiose:quinone oxidoreductase. As with CDH from wood-rotting fungi, the intact, monomeric enzyme from S. rolfsii contains one heme b and one flavin adenine dinucleotide cofactor per molecule. It has a molecular size of 101 kDa, of which 15% is glycosylation, and a pI value of 4.2. The preferred substrates are cellobiose and cellooligosaccharides; additionally, ␤-lactose, thiocellobiose, and xylobiose are efficiently oxidized. Cytochrome c (equine) and the azino-di-(3-ethyl-benzthiazolin-6-sulfonic acid) cation radical were the best electron acceptors, while DCIP, 1,4-benzoquinone, phenothiazine dyes such as methylene blue, phenoxazine dyes such as Meldola's blue, and ferricyanide were also excellent acceptors. In addition, electrons can be transferred to oxygen. Limited in vitro proteolysis with papain resulted in the formation of several protein fragments that are active with DCIP but not with cytochrome c. Such a flavin-containing fragment, with a mass of 75 kDa and a pI of 5.1 and lacking the heme domain, was isolated and partially characterized.

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Isolation and Characterization of the Cellobiose Dehydrogenase from the Brown-Rot Fungus Coniophora puteana (Schum ex Fr.) Karst.

Cited by 53 publications

References 0 publications

Plant-Polysaccharide-Degrading Enzymes from Basidiomycetes

Plant-Polysaccharide-Degrading Enzymes from Basidiomycetes

A Mechanism for Production of Hydroxyl Radicals by the Brown-Rot Fungus Coniophora Puteana: Fe(III) Reduction by Cellobiose Dehydrogenase and Fe(II) Oxidation at a Distance from the Hyphae

Purification and Characterization of Cellobiose Dehydrogenase from the Plant PathogenSclerotium(Athelia)rolfsii

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