Characterization of the Two Neurospora crassa Cellobiose Dehydrogenases and Their Connection to Oxidative Cellulose Degradation

Sygmund, Christoph; Kracher, Daniel; Scheiblbrandner, Stefan; Zahma, Kawah; Felice, Alfons K. G.; Harreither, Wolfgang; Kittl, Roman; Ludwig, Roland

doi:10.1128/aem.01503-12

Cited by 117 publications

(133 citation statements)

References 42 publications

(59 reference statements)

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“…The ascomycete CDHs isolated from N. crassa have a broader substrate spectrum and less glucose discrimination than basidiomycete CDHs (30). While basidiomycete CDHs catalyze the reactions at acidic pH, ascomycete CDHs are active at neutral or alkaline pH (41). Whether the differences in the biochemical characteristics of CDHs between basidiomycetes and ascomycetes are also valid for Aspergillus species remains to be clarified.…”

Section: Cellulose-degrading Enzymesmentioning

confidence: 99%

“…First, the ability of CDH to accept electrons from xylooligosaccharides and interact with various LPMOs was detected, suggesting that these enzymes are able to act on hemicelluloses (41). Recently, LPMO9C of the ascomycete fungus Neurospora crassa was shown to cleave xyloglucan, ␤-glucan, and, to a lesser extent, glucomannan with ascorbic acid as a reductant (40).…”

Section: Hemicellulose Degradationmentioning

confidence: 99%

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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 Enzymesmentioning

confidence: 99%

Section: Hemicellulose Degradationmentioning

confidence: 99%

Plant-Polysaccharide-Degrading Enzymes from Basidiomycetes

Rytioja

Hildén

Yuzon

et al. 2014

Microbiol Mol Biol Rev

348

287

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“…Recent studies demonstrated that LPMOs act in concert with CDH since their association resulted in an increase in the conversion of cellulose, assuming a key role of this oxidative system in fungi (8,11,12,31). The effectiveness of LPMO/CDH synergy seems to depend on enzyme concentrations and the type of substrate used.…”

mentioning

confidence: 99%

Cello-Oligosaccharide Oxidation Reveals Differences between Two Lytic Polysaccharide Monooxygenases (Family GH61) from Podospora anserina

Bey

Zhou

Poidevin

et al. 2013

Appl Environ Microbiol

159

151

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The genome of the coprophilic ascomycete Podospora anserina encodes 33 different genes encoding copper-dependent lytic polysaccharide monooxygenases (LPMOs) from glycoside hydrolase family 61 (GH61). In this study, two of these enzymes (P. anserina GH61A [PaGH61A] and PaGH61B), which both harbored a family 1 carbohydrate binding module, were successfully produced in Pichia pastoris. Synergistic cooperation between PaGH61A or PaGH61B with the cellobiose dehydrogenase (CDH) of Pycnoporus cinnabarinus on cellulose resulted in the formation of oxidized and nonoxidized cello-oligosaccharides. A striking difference between PaGH61A and PaGH61B was observed through the identification of the products, among which were doubly and triply oxidized cellodextrins, which were released only by the combination of PaGH61B with CDH. The mass spectrometry fragmentation patterns of these oxidized products could be consistent with oxidation at the C-6 position with a geminal diol group. The different properties of PaGH61A and PaGH61B and their effect on the interaction with CDH are discussed in regard to the proposed in vivo function of the CDH/GH61 enzyme system in oxidative cellulose hydrolysis.

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“…Nevertheless, their actual function is still not fully understood (1,9,15,16). Recently, fungal CDHs were shown to act as a reductant for lytic polysaccharide mono-oxygenases (LPMOs), providing electrons for the redox-mediated oxidative cleavage of cellulose (14,17,(21)(22)(23). The electrons are rapidly transferred from the flavin to the heme domain of CDH via the heme propionate group (24)(25)(26).…”

mentioning

confidence: 99%

“…The first CDHs, initially named cellobiose oxidase, were discovered as enzymes able to catalyze the cellobiose-dependent reduction of quinones (5,6). Their enzymatic properties have been characterized in many fungi, including Phanerochaete chrysosporium (7), Trametes versicolor (8), Schizophyllum commune (9), Pycnoporus cinnabarinus (3), Pycnoporus sanguineus (10), Cerrena unicolor (11), Podospora anserina (12,13), and Neurospora crassa (14)(15)(16)(17). Zámocký et al (18) divided the CDH family into three phylogenetic branches.…”

mentioning

confidence: 99%

Inactivation of Cellobiose Dehydrogenases Modifies the Cellulose Degradation Mechanism of Podospora anserina

Tangthirasunun

Navarro

Garajová

et al. 2017

Appl Environ Microbiol

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Conversion of biomass into high-value products, including biofuels, is of great interest to developing sustainable biorefineries. Fungi are an inexhaustible source of enzymes to degrade plant biomass. Cellobiose dehydrogenases (CDHs) play an important role in the breakdown through synergistic action with fungal lytic polysaccharide monooxygenases (LPMOs). The three CDH genes of the model fungus Podospora anserina were inactivated, resulting in single and multiple CDH mutants. We detected almost no difference in growth and fertility of the mutants on various lignocellulose sources, except on crystalline cellulose, on which a 2-fold decrease in fertility of the mutants lacking P. anserina CDH1 (PaCDH1) and PaCDH2 was observed. A striking difference between wild-type and mutant secretomes was observed. The secretome of the mutant lacking all CDHs contained five beta-glucosidases, whereas the wild type had only one. P. anserina seems to compensate for the lack of CDH with secretion of beta-glucosidases. The addition of P. anserina LPMO to either the wild-type or mutant secretome resulted in improvement of cellulose degradation in both cases, suggesting that other redox partners present in the mutant secretome provided electrons to LPMOs. Overall, the data showed that oxidative degradation of cellulosic biomass relies on different types of mechanisms in fungi.IMPORTANCE Plant biomass degradation by fungi is a complex process involving dozens of enzymes. The roles of each enzyme or enzyme class are not fully understood, and utilization of a model amenable to genetic analysis should increase the comprehension of how fungi cope with highly recalcitrant biomass. Here, we report that the cellobiose dehydrogenases of the model fungus Podospora anserina enable it to consume crystalline cellulose yet seem to play a minor role on actual substrates, such as wood shavings or miscanthus. Analysis of secreted proteins suggests that Podospora anserina compensates for the lack of cellobiose dehydrogenase by increasing beta-glucosidase expression and using an alternate electron donor for LPMO.

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Characterization of the Two Neurospora crassa Cellobiose Dehydrogenases and Their Connection to Oxidative Cellulose Degradation

Cited by 117 publications

References 42 publications

Plant-Polysaccharide-Degrading Enzymes from Basidiomycetes

Plant-Polysaccharide-Degrading Enzymes from Basidiomycetes

Cello-Oligosaccharide Oxidation Reveals Differences between Two Lytic Polysaccharide Monooxygenases (Family GH61) from Podospora anserina

Inactivation of Cellobiose Dehydrogenases Modifies the Cellulose Degradation Mechanism of Podospora anserina

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