Characterization of a cellobiose dehydrogenase in the cellulolytic fungus <i>Sporotrichum (Chrysosporium)</i> thermophile

Coudray, M R; Canevascini, Giorgio; Meier, Hans

doi:10.1042/bj2030277

Cited by 74 publications

(25 citation statements)

References 23 publications

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“…The absorption spectra of the enzyme indicated the presence of neither a heme nor an FAD group. Since the catalytic properties of the enzyme were similar to those of the first described cellobiose dehydrogenases (13,15)-at that time a term commonly used for the flavin-only enzyme-it also was termed cellobiose dehydrogenase, and it was speculated that it might possibly carry a different cofactor.…”

Section: Discussionmentioning

confidence: 99%

“…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).…”

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confidence: 99%

“…Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was carried out on an Amersham-Pharmacia Multiphor II system using precast ExcelGel SDS gradient gels (8)(9)(10)(11)(12)(13)(14)(15)(16)(17)(18). Native PAGE was carried out on an Amersham-Pharmacia Phast System using precast PhastGel gradient gels (8-25) with both high-and low-molecular-weight standards (Amersham-Pharmacia).…”

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confidence: 99%

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

Baminger

Subramaniam

Renganathan

et al. 2001

Appl Environ Microbiol

122

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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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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

Baminger

Subramaniam

Renganathan

et al. 2001

Appl Environ Microbiol

122

108

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“…These properties suggested that the enzyme VOL. 64,2000 PHYSIOLOGY AND ENZYMES OF THERMOPHILIC FUNGI 477…”

Section: Laccasementioning

confidence: 99%

Thermophilic Fungi: Their Physiology and Enzymes

Maheshwari

Bharadwaj

Bhat

2000

Microbiol Mol Biol Rev

658

380

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SUMMARY Thermophilic fungi are a small assemblage in mycota that have a minimum temperature of growth at or above 20°C and a maximum temperature of growth extending up to 60 to 62°C. As the only representatives of eukaryotic organisms that can grow at temperatures above 45°C, the thermophilic fungi are valuable experimental systems for investigations of mechanisms that allow growth at moderately high temperature yet limit their growth beyond 60 to 62°C. Although widespread in terrestrial habitats, they have remained underexplored compared to thermophilic species of eubacteria and archaea. However, thermophilic fungi are potential sources of enzymes with scientific and commercial interests. This review, for the first time, compiles information on the physiology and enzymes of thermophilic fungi. Thermophilic fungi can be grown in minimal media with metabolic rates and growth yields comparable to those of mesophilic fungi. Studies of their growth kinetics, respiration, mixed-substrate utilization, nutrient uptake, and protein breakdown rate have provided some basic information not only on thermophilic fungi but also on filamentous fungi in general. Some species have the ability to grow at ambient temperatures if cultures are initiated with germinated spores or mycelial inoculum or if a nutritionally rich medium is used. Thermophilic fungi have a powerful ability to degrade polysaccharide constituents of biomass. The properties of their enzymes show differences not only among species but also among strains of the same species. Their extracellular enzymes display temperature optima for activity that are close to or above the optimum temperature for the growth of organism and, in general, are more heat stable than those of the mesophilic fungi. Some extracellular enzymes from thermophilic fungi are being produced commercially, and a few others have commercial prospects. Genes of thermophilic fungi encoding lipase, protease, xylanase, and cellulase have been cloned and overexpressed in heterologous fungi, and pure crystalline proteins have been obtained for elucidation of the mechanisms of their intrinsic thermostability and catalysis. By contrast, the thermal stability of the few intracellular enzymes that have been purified is comparable to or, in some cases, lower than that of enzymes from the mesophilic fungi. Although rigorous data are lacking, it appears that eukaryotic thermophily involves several mechanisms of stabilization of enzymes or optimization of their activity, with different mechanisms operating for different enzymes.

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“…CDH activity was reported in cultures of the ascomycetes Thielavia heterothallica (synonyms, Myceliophthora thermophila and Sporotrichum thermophile) (3,4), Chaetomium sp. INBI 2-26(Ϫ) (38), Chaetomium cellulolyticum (10), Neurospora crassa (11), Humicola insolens (32), and Myriococcum thermophilum (14).…”

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Catalytic Properties and Classification of Cellobiose Dehydrogenases from Ascomycetes

Harreither

Sygmund

Augustin

et al. 2011

Appl Environ Microbiol

131

102

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Putative cellobiose dehydrogenase (CDH) genes are frequently discovered in various fungi by genome sequencing projects. The expression of CDH, an extracellular flavocytochrome, is well studied in white rot basidiomycetes and is attributed to extracellular lignocellulose degradation. CDH has also been reported for plant-pathogenic or saprotrophic ascomycetes, but the molecular and catalytic properties of these enzymes are currently less investigated. This study links various ascomycetous cdh genes with the molecular and catalytic characteristics of the mature proteins and suggests a differentiation of ascomycete class II CDHs into two subclasses, namely, class IIA and class IIB, in addition to the recently introduced class III of hypothetical ascomycete CDHs. This new classification is based on sequence and biochemical data obtained from sequenced fungal genomes and a screening of 40 ascomycetes. Thirteen strains showed CDH activity when they were grown on cellulose-based media, and Chaetomium atrobrunneum, Corynascus thermophilus, Dichomera saubinetii, Hypoxylon haematostroma, Neurospora crassa, and Stachybotrys bisbyi were selected for detailed studies. In these strains, one or two cdh-encoding genes were found that stem either from class IIA and contain a C-terminal carbohydrate-binding module or from class IIB without such a module. In several strains, both genes were found. Regarding substrate specificity, class IIB CDHs show a less pronounced substrate specificity for cellobiose than class IIA enzymes. A pH-dependent pattern of the intramolecular electron transfer was also observed, and the CDHs were classified into three groups featuring acidic, intermediate, or alkaline pH optima. The pH optimum, however, does not correlate with the CDH subclasses and is most likely a species-dependent adaptation to different habitats.

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Characterization of a cellobiose dehydrogenase in the cellulolytic fungus Sporotrichum (Chrysosporium) thermophile

Cited by 74 publications

References 23 publications

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

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

Thermophilic Fungi: Their Physiology and Enzymes

Catalytic Properties and Classification of Cellobiose Dehydrogenases from Ascomycetes

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