Cellobiose Dehydrogenase and a Copper-Dependent Polysaccharide Monooxygenase Potentiate Cellulose Degradation by Neurospora crassa

2011 ◽  
Vol 6 (12) ◽  
pp. 1399-1406 ◽  
Author(s):  
Christopher M. Phillips ◽  
William T. Beeson ◽  
Jamie H. Cate ◽  
Michael A. Marletta
2012 ◽  
Vol 78 (17) ◽  
pp. 6161-6171 ◽  
Author(s):  
Christoph Sygmund ◽  
Daniel Kracher ◽  
Stefan Scheiblbrandner ◽  
Kawah Zahma ◽  
Alfons K. G. Felice ◽  
...  

ABSTRACTThe genome ofNeurospora crassaencodes two different cellobiose dehydrogenases (CDHs) with a sequence identity of only 53%. So far, only CDH IIA, which is induced during growth on cellulose and features a C-terminal carbohydrate binding module (CBM), was detected in the secretome ofN. crassaand preliminarily characterized. CDH IIB is not significantly upregulated during growth on cellulosic material and lacks a CBM. Since CDH IIB could not be identified in the secretome, both CDHs were recombinantly produced inPichia pastoris. With the cytochrome domain-dependent one-electron acceptor cytochromec, CDH IIA has a narrower and more acidic pH optimum than CDH IIB. Interestingly, the catalytic efficiencies of both CDHs for carbohydrates are rather similar, but CDH IIA exhibits 4- to 5-times-higher apparent catalytic constants (kcatandKmvalues) than CDH IIB for most tested carbohydrates. A third major difference is the 65-mV-lower redox potential of the hemebcofactor in the cytochrome domain of CDH IIA than CDH IIB. To study the interaction with a member of the glycoside hydrolase 61 family, the copper-dependent polysaccharide monooxygenase GH61-3 (NCU02916) fromN. crassawas expressed inP. pastoris. A pH-dependent electron transfer from both CDHs via their cytochrome domains to GH61-3 was observed. The different properties of CDH IIA and CDH IIB and their effect on interactions with GH61-3 are discussed in regard to the proposedin vivofunction of the CDH/GH61 enzyme system in oxidative cellulose hydrolysis.


FEBS Journal ◽  
2019 ◽  
Vol 287 (5) ◽  
pp. 897-908 ◽  
Author(s):  
Daniel Kracher ◽  
Zarah Forsberg ◽  
Bastien Bissaro ◽  
Sonja Gangl ◽  
Marita Preims ◽  
...  

2016 ◽  
Vol 67 (3) ◽  
pp. 145-163 ◽  
Author(s):  
Daniel Kracher ◽  
Roland Ludwig

SummaryThe flavin and heme cofactor containing enzyme cellobiose dehydrogenase (CDH) is ubiquitously distributed in wood-degrading fungi. Current research provides compelling evidence that CDH is an activator for cellulolytic monooxygenases, which enhance the accessibility of crystalline cellulose surfaces for hydrolases. Such oxidative cellulose degradation contributes to the overall cellulolytic capabilities of wood decaying fungi to a large extent, and holds great potential to improve the efficiency of commercial enzyme mixtures for biomass processing and biofuel production. This review summarizes current literature with regard to the distribution, structure and physiological role of CDH in the light of recent findings.


2014 ◽  
Vol 80 (7) ◽  
pp. 2062-2070 ◽  
Author(s):  
Chiaki Hori ◽  
Jill Gaskell ◽  
Kiyohiko Igarashi ◽  
Phil Kersten ◽  
Michael Mozuch ◽  
...  

ABSTRACTThe white-rot basidiomycetes efficiently degrade all wood cell wall polymers. Generally, these fungi simultaneously degrade cellulose and lignin, but certain organisms, such asCeriporiopsis subvermispora, selectively remove lignin in advance of cellulose degradation. However, relatively little is known about the mechanism of selective ligninolysis. To address this issue,C. subvermisporawas grown in liquid medium containing ball-milled aspen, and nano-liquid chromatography-tandem mass spectrometry was used to identify and estimate extracellular protein abundance over time. Several manganese peroxidases and an aryl alcohol oxidase, both associated with lignin degradation, were identified after 3 days of incubation. A glycoside hydrolase (GH) family 51 arabinofuranosidase was also identified after 3 days but then successively decreased in later samples. Several enzymes related to cellulose and xylan degradation, such as GH10 endoxylanase, GH5_5 endoglucanase, and GH7 cellobiohydrolase, were detected after 5 days. Peptides corresponding to potential cellulose-degrading enzymes GH12, GH45, lytic polysaccharide monooxygenase, and cellobiose dehydrogenase were most abundant after 7 days. This sequential production of enzymes provides a mechanism consistent with selective ligninolysis byC. subvermispora.


Holzforschung ◽  
2005 ◽  
Vol 59 (3) ◽  
pp. 263-268 ◽  
Author(s):  
Martin Kruså ◽  
Gunnar Henriksson ◽  
Gunnar Johansson ◽  
Torbjörn Reitberger ◽  
Helena Lennholm

AbstractCellobiose dehydrogenase (CDH) is an extracellular enzyme produced by various wood-degrading fungi. It oxidizes cellobiose to cellobionolactone under reduction of molecular oxygen to hydrogen peroxide, and Fe3+to Fe2+. These activated agents can thereafter form highly reactive hydroxyl radicals, which depolymerize wood polymers. In this work, cellulose depolymerization by CDH was studied using a model compound, methyl β-D-glucopyranoside. The formation of glucose, arabinose, gluconic acid, erythrulose and formaldehyde were detected and a mechanism for the reaction is proposed. The biological importance of this enzyme-initiated reaction is discussed.


2020 ◽  
Author(s):  
Bjørge Westereng ◽  
Stjepan K. Kračun ◽  
Shaun Leivers ◽  
Magnus Ø. Arntzen ◽  
Finn L. Aachmann ◽  
...  

ABSTRACTPolysaccharides from plant biomass are the most abundant renewable chemicals on Earth and can potentially be converted to a wide variety of useful glycoconjugates. While anomeric hydroxyl groups of carbohydrates are amenable to a variety of useful chemical modifications, selective cross-coupling to non-reducing ends has remained challenging. Several lytic polysaccharide monooxygenases (LPMOs), powerful enzymes known for their application in cellulose degradation, specifically oxidize non-reducing ends, introducing carbonyl groups that can be utilized for chemical coupling. This study provides a simple and highly specific approach to produce oxime-based glycoconjugates from LPMO-functionalized oligosaccharides. The products are evaluated by HPLC, mass spectrometry and NMR. Furthermore, we demonstrate potential biodegradability of these glycoconjugates using selective enzymes.


1998 ◽  
Vol 64 (5) ◽  
pp. 1924-1928 ◽  
Author(s):  
Marcelo A. Vallim ◽  
Bernard J. H. Janse ◽  
Jill Gaskell ◽  
Aline A. Pizzirani-Kleiner ◽  
Daniel Cullen

ABSTRACT The transcripts of structurally related cellobiohydrolase genes inPhanerochaete chrysosporium-colonized wood chips were quantified. The transcript patterns obtained were dramatically different from the transcript patterns obtained previously in defined media. Cellobiose dehydrogenase transcripts were also detected, which is consistent with the hypothesis that such transcripts play an important role in cellulose degradation.


Biochemistry ◽  
2019 ◽  
Vol 58 (9) ◽  
pp. 1226-1235 ◽  
Author(s):  
Christophe V. F. P. Laurent ◽  
Erik Breslmayr ◽  
Daniel Tunega ◽  
Roland Ludwig ◽  
Chris Oostenbrink

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