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Journal articles on the topic 'Cellobiose dehydrogenase'

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Published: 4 June 2021

Last updated: 15 June 2025

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1

SCHOU, Charlotte, H. Margrethe CHRISTENSEN, and Martin SCHÜLEIN. "Characterization of a cellobiose dehydrogenase from Humicola insolens." Biochemical Journal 330, no. 1 (1998): 565–71. http://dx.doi.org/10.1042/bj3300565.

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The major cellobiose dehydrogenase (oxidase) (CBDH) secreted by the soft-rot thermophilic fungus Humicola insolens during growth on cellulose has been isolated and purified. It was shown to be a haemoflavoprotein with a molecular weight of 92 kDa and a pI of 4.0, capable of oxidizing the anomeric carbon of cellobiose, soluble cellooligosaccharides, lactose, xylobiose and maltose. Possible electron acceptors are 2,6-dichlorophenol-indophenol (DCPIP), Methylene Blue, 3,5-di-t-butyl-1,2-benzoquinone, potassium ferricyanide, cytochrome c and molecular oxygen. The oxidation of the prosthetic groups by oxygen was monitored at 449 nm for the flavin group and at 562 nm for the haem group. The curves were very similar to those of the cellobiose dehydrogenase from Phanerochaete chrysosporium, suggesting a similar mechanism. The pH-optima for the oxidation varied remarkably depending on the electron acceptor. For the organic electron acceptors, the pH-optima ranged from pH 4 for Methylene Blue to pH 7 for DCPIP and the benzoquinone. In the case of the FeIII-containing electron acceptors, the enzyme displayed alkaline pH-optima, in contrast to the properties of cellobiose dehydrogenases from Phanerochaete chrysosporium and Myceliophthora (Sporotrichum) thermophila. The enzyme has optimal activity at 65 °C.

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2

Scheiblbrandner, Stefan, Florian Csarman, and Roland Ludwig. "Cellobiose dehydrogenase in biofuel cells." Current Opinion in Biotechnology 73 (February 2022): 205–12. http://dx.doi.org/10.1016/j.copbio.2021.08.013.

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3

Tegl, Gregor, Barbara Thallinger, Bianca Beer, et al. "Antimicrobial Cellobiose Dehydrogenase-Chitosan Particles." ACS Applied Materials & Interfaces 8, no. 1 (2015): 967–73. http://dx.doi.org/10.1021/acsami.5b10801.

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4

Nyanhongo, Gibson S., Barbara Thallinger, and Georg M. Guebitz. "Cellobiose dehydrogenase-based biomedical applications." Process Biochemistry 59 (August 2017): 37–45. http://dx.doi.org/10.1016/j.procbio.2017.02.023.

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5

Schimz, Karl-L., and Gaby Decker. "Cellobiose phosphorylase (EC 2.4.1.20) of Cellulomonas sp.: investigations on its localization." Canadian Journal of Microbiology 31, no. 8 (1985): 751–54. http://dx.doi.org/10.1139/m85-140.

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Cells of Cellulomonas sp. (DSM 20108) grown with cellobiose as sole source of energy and carbon, and containing induced cellobiose phosphorylase activity, were disrupted for various lengths of time by ultrasonication and by lysozyme treatment. The cytosol and particulate fractions were prepared by ultracentrifugation (105 000 × g, 1 h, 8 °C). Protein concentration as well as activities of several marker enzymes (hexokinase, D-glucose-6-phosphate dehydrogenase, and 6-phospho-D-gluconate dehydrogenase) and of cellobiose phosphorylase were determined and their time-dependent increase in the cytosol and pellet fractions was compared. The occurrence of D-glucose-6-phosphate dehydrogenase in the 105 000 × g pellet during lysozyme treatment was shown to be caused by coprecipitation with lysozyme. From the results obtained it is concluded that cellobiose phosphorylase of Cellulomonas sp. is localized in the soluble cytosol fraction.

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6

Cameron, Michael D., and Steven D. Aust. "Cellobiose dehydrogenase–an extracellular fungal flavocytochrome." Enzyme and Microbial Technology 28, no. 2-3 (2001): 129–38. http://dx.doi.org/10.1016/s0141-0229(00)00307-0.

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7

Scheiblbrandner, Stefan, and Roland Ludwig. "Cellobiose dehydrogenase: Bioelectrochemical insights and applications." Bioelectrochemistry 131 (February 2020): 107345. http://dx.doi.org/10.1016/j.bioelechem.2019.107345.

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8

Morpeth, F. F., and G. D. Jones. "Resolution, purification and some properties of the multiple forms of cellobiose quinone dehydrogenase from the white-rot fungus Sporotrichum pulverulentum." Biochemical Journal 236, no. 1 (1986): 221–26. http://dx.doi.org/10.1042/bj2360221.

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Four forms of cellobiose quinone dehydrogenase have been purified from the white-rot fungus Sporotrichum pulverulentum. The Mr of the enzyme has been estimated by sedimentation equilibrium to be 57,800 and by SDS/polyacrylamide-gel to be 60,000. These enzymes are clearly monomers. Cellobiose quinone dehydrogenases contain FAD and variable amounts of a green chromophore which we suggest is 6-hydroxy-FAD. The superoxide anion and H2O2 are the products of its reaction with oxygen. All of the isoenzymes from any one preparation display similar kinetic parameters. However, these vary between preparations. The only apparent difference between the four separable isoenzymes is their neutral-sugar content.

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9

Fridman, V., U. Wollenberger, V. Bogdanovskaya, et al. "Electrochemical investigation of cellobiose oxidation by cellobiose dehydrogenase in the presence of cytochrome c as mediator." Biochemical Society Transactions 28, no. 2 (2000): 63–70. http://dx.doi.org/10.1042/bst0280063.

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An important aspect of the cytochrome c electrochemistry is the possibility of coupling the ‘heterogeneous reactions’ with other redox enzymes. Cellobiose dehydrogenase, a 89170 Da glycoprotein that contains both FAD and a b-type haem as prosthetic groups, donates electrons to a number of acceptors, including cytochrome c. While haem b is surrounded mainly by acidic amino acids, cytochrome c displays positive charged lysine groups around the haem site. Thus a fast reaction between both proteins is explicable. In the presence of cellobiose, a catalytic current was observed, owing to the interaction of cellobiose dehydrogenase with electrostatically adsorbed cytochrome c. Adsorption of cytochrome c provides a technological model surface for vectorial electron transfer.

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10

Kim, Eun-Ji, Seong-Woo Kang, Kwang-Ho Song, Sung-Ok Han, Jae-Jin Kim та Seung-Wook Kim. "Improvement of Cellobiose Dehydrogenase(CDH) and β-Glucosidase Activity by Phanerochaete chrysosporium Mutant". Korean Chemical Engineering Research 49, № 1 (2011): 101–4. http://dx.doi.org/10.9713/kcer.2011.49.1.101.

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11

Canevascini, Giorgio. "A cellulase assay coupled to cellobiose dehydrogenase." Analytical Biochemistry 147, no. 2 (1985): 419–27. http://dx.doi.org/10.1016/0003-2697(85)90291-x.

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12

Igarashi, Kiyohiko, Marc F. J. M. Verhagen, Masahiro Samejima, Martin Schülein, Karl-Erik L. Eriksson, and Takeshi Nishino. "Cellobiose Dehydrogenase from the FungiPhanerochaete chrysosporiumandHumicola insolens." Journal of Biological Chemistry 274, no. 6 (1999): 3338–44. http://dx.doi.org/10.1074/jbc.274.6.3338.

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13

Stapleton, P. C., J. O'Mahony, and A. D. W. Dobson. "Real-time PCR analysis of carbon catabolite repression of cellobiose dehydrogenase gene transcription inTrametes versicolor." Canadian Journal of Microbiology 50, no. 2 (2004): 113–19. http://dx.doi.org/10.1139/w03-108.

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Cellobiose dehydrogenase production in Trametes versicolor is repressed when additional carbon sources, such as glucose, maltose, galactose, arabinose, and xylose, are added to the fungal cultures growing on cellulose. Real-time quantitative reverse transcription – polymerase chain reaction has been used to demonstrate that the addition of galactose, arabinose, and xylose results in 19-, 92-, and 114-fold reductions, respectively, in cdh transcript levels 96 h post-addition. Glucose exhibits the greatest repressive effect, resulting in a 3400-fold decrease in cdh transcript levels.Key words: cellobiose dehydrogenase, carbon repression, real-time PCR.

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14

Mulla, Dafina, Daniel Kracher, Roland Ludwig, et al. "Azido derivatives of cellobiose: oxidation at C1 with cellobiose dehydrogenase from Sclerotium rolfsii." Carbohydrate Research 382 (December 2013): 86–94. http://dx.doi.org/10.1016/j.carres.2013.09.004.

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15

Karapetyan, K. N., T. V. Fedorova, L. G. Vasil’chenko, R. Ludwig, D. Haltrich, and M. L. Rabinovich. "Properties of neutral cellobiose dehydrogenase from the ascomycete Chaetomium sp. INBI 2-26(–) and comparison with basidiomycetous cellobiose dehydrogenases." Journal of Biotechnology 121, no. 1 (2006): 34–48. http://dx.doi.org/10.1016/j.jbiotec.2005.06.024.

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16

Lisov, Alexander V., Oksana V. Belova, Nataliya G. Vinokurova, Tatiana V. Semashko, Anatolii G. Lobanok та Alexey A. Leontievsky. "Transformation of cellobiose during the interaction of cellobiose dehydrogenase and β-glucosidase ofCerrena unicolor". Journal of Basic Microbiology 58, № 4 (2018): 322–30. http://dx.doi.org/10.1002/jobm.201700399.

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17

Olszewska, Katarzyna, Anna Olszewska, Jerzy Rogalski, and Justyna Sulej. "BIOTECHNOLOGICAL AND BIOMEDICAL APPLICATIONS OF FUNGAL CELLOBIOSE DEHYDROGENASE." Postępy Mikrobiologii - Advancements of Microbiology 59, no. 1 (2020): 75–86. http://dx.doi.org/10.21307/pm-2020.59.1.007.

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18

Harreither, Wolfgang, Christoph Sygmund, Evelyn Dünhofen, Rafael Vicuña, Dietmar Haltrich, and Roland Ludwig. "Cellobiose Dehydrogenase from the Ligninolytic Basidiomycete Ceriporiopsis subvermispora." Applied and Environmental Microbiology 75, no. 9 (2009): 2750–57. http://dx.doi.org/10.1128/aem.02320-08.

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ABSTRACT Cellobiose dehydrogenase (CDH), an extracellular flavocytochrome produced by several wood-degrading fungi, was detected in cultures of the selective delignifier Ceriporiopsis subvermispora when grown on a cellulose- and yeast extract-based liquid medium. CDH amounted to up to 2.5% of total extracellular protein during latter phases of the cultivation and thus suggested an important function for the fungus under the given conditions. The enzyme was purified 44-fold to apparent homogeneity. It was found to be present in two glycoforms of 98 kDa and 87 kDa with carbohydrate contents of 16 and 4%, respectively. The isoelectric point of both glycoforms is around 3.0, differing by 0.1 units, which is the most acidic value so far reported for a CDH. By using degenerated primers of known CDH sequences, one cdh gene was found in the genomic DNA, cloned, and sequenced. Alignment of the 774-amino-acid protein sequence revealed a high similarity to CDH from other white rot fungi. One notable difference was found in the longer interdomain peptide linker, which might affect the interdomain electron transfer at higher temperatures. The preferred substrate of C. subvermispora CDH is cellobiose, while glucose conversion is strongly discriminated by a 155,000-fold-lower catalytic efficiency. This is a typical feature of a basidiomycete CDH, as are the acidic pH optima for all tested electron acceptors in the range from 2.5 to 4.5.

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19

Laurent, Christophe V. F. P., Erik Breslmayr, Daniel Tunega, Roland Ludwig, and Chris Oostenbrink. "Interaction between Cellobiose Dehydrogenase and Lytic Polysaccharide Monooxygenase." Biochemistry 58, no. 9 (2019): 1226–35. http://dx.doi.org/10.1021/acs.biochem.8b01178.

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20

Moukha, S. M., T. J. Dumonceaux, E. Record, and F. S. Archibald. "Cloning and analysis of Pycnoporus cinnabarinus cellobiose dehydrogenase." Gene 234, no. 1 (1999): 23–33. http://dx.doi.org/10.1016/s0378-1119(99)00189-4.

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21

Henriksson, Gunnar, Veljo Sild, István J. Szabó, Göran Pettersson, and Gunnar Johansson. "Substrate specificity of cellobiose dehydrogenase from Phanerochaete chrysosporium." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1383, no. 1 (1998): 48–54. http://dx.doi.org/10.1016/s0167-4838(97)00180-5.

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22

Larsson, Ted, Maja Elmgren, Sten-Eric Lindquist, Merid Tessema, Lo Gorton, and Gunnar Henriksson. "Electron transfer between cellobiose dehydrogenase and graphite electrodes." Analytica Chimica Acta 331, no. 3 (1996): 207–15. http://dx.doi.org/10.1016/0003-2670(96)00136-5.

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23

Mansfield, S. D., E. De Jong, and J. N. Saddler. "Cellobiose dehydrogenase, an active agent in cellulose depolymerization." Applied and environmental microbiology 63, no. 10 (1997): 3804–9. http://dx.doi.org/10.1128/aem.63.10.3804-3809.1997.

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24

Vallim, Marcelo A., Bernard J. H. Janse, Jill Gaskell, Aline A. Pizzirani-Kleiner, and Daniel Cullen. "Phanerochaete chrysosporiumCellobiohydrolase and Cellobiose Dehydrogenase Transcripts in Wood." Applied and Environmental Microbiology 64, no. 5 (1998): 1924–28. http://dx.doi.org/10.1128/aem.64.5.1924-1928.1998.

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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.

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25

Sulej, Justyna, Grzegorz Janusz, Andrzej Mazur, Karolina Żuber, Anna Żebracka, and Jerzy Rogalski. "Cellobiose dehydrogenase from the ligninolytic basidiomycete Phlebia lindtneri." Process Biochemistry 48, no. 11 (2013): 1715–23. http://dx.doi.org/10.1016/j.procbio.2013.08.003.

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26

Jensen, Uffe Bjørnholt, Hossein Mohammad‐Beigi, Stepan Shipovskov, Duncan S. Sutherland, and Elena E. Ferapontova. "Activation of Cellobiose Dehydrogenase Bioelectrocatalysis by Carbon Nanoparticles." ChemElectroChem 6, no. 19 (2019): 5032–40. http://dx.doi.org/10.1002/celc.201901066.

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27

Ludwig, Roland, Wolfgang Harreither, Federico Tasca, and Lo Gorton. "Cellobiose Dehydrogenase: A Versatile Catalyst for Electrochemical Applications." ChemPhysChem 11, no. 13 (2010): 2674–97. http://dx.doi.org/10.1002/cphc.201000216.

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28

Stevenson, David M., and Paul J. Weimer. "Expression of 17 Genes in Clostridium thermocellum ATCC 27405 during Fermentation of Cellulose or Cellobiose in Continuous Culture." Applied and Environmental Microbiology 71, no. 8 (2005): 4672–78. http://dx.doi.org/10.1128/aem.71.8.4672-4678.2005.

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ABSTRACT Clostridium thermocellum is a thermophilic, anaerobic, cellulolytic bacterium that produces ethanol and acetic acid as major fermentation end products. The effect of growth conditions on gene expression in C. thermocellum ATCC 27405 was studied using cells grown in continuous culture under cellobiose or cellulose limitation over a ∼10-fold range of dilution rates (0.013 to 0.16 h−1). Fermentation product distribution displayed similar patterns in cellobiose- or cellulose-grown cultures, including substantial shifts in the proportion of ethanol and acetic acid with changes in growth rate. Expression of 17 genes involved or potentially involved in cellulose degradation, intracellular phosphorylation, catabolite repression, and fermentation end product formation was quantified by real-time PCR, with normalization to two calibrator genes (recA and the 16S rRNA gene) to determine relative expression. Thirteen genes displayed modest (fivefold or less) differences in expression with growth rate or substrate type: sdbA (cellulosomal scaffoldin-dockerin binding protein), cdp (cellodextrin phosphorylase), cbp (cellobiose phosphorylase), hydA (hydrogenase), ldh (lactate dehydrogenase), ack (acetate kinase), one putative type IV alcohol dehydrogenase, two putative cyclic AMP binding proteins, three putative Hpr-like proteins, and a putative Hpr serine kinase. By contrast, four genes displayed >10-fold-reduced levels of expression when grown on cellobiose at dilution rates of >0.05 h−1: cipA (cellulosomal scaffolding protein), celS (exoglucanase), manA (mannanase), and a second type IV alcohol dehydrogenase. The data suggest that at least some cellulosomal components are transcriptionally regulated but that differences in expression with growth rate or among substrates do not directly account for observed changes in fermentation end product distribution.

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29

Bozorgzadeh, Somayyeh, Hassan Hamidi, Roberto Ortiz, Roland Ludwig, and Lo Gorton. "Direct electron transfer of Phanerochaete chrysosporium cellobiose dehydrogenase at platinum and palladium nanoparticles decorated carbon nanotubes modified electrodes." Physical Chemistry Chemical Physics 17, no. 37 (2015): 24157–65. http://dx.doi.org/10.1039/c5cp03812j.

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30

Hildebrand, Amanda, Edyta Szewczyk, Hui Lin, Takao Kasuga, and Zhiliang Fan. "Engineering Neurospora crassa for Improved Cellobiose and Cellobionate Production." Applied and Environmental Microbiology 81, no. 2 (2014): 597–603. http://dx.doi.org/10.1128/aem.02885-14.

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ABSTRACTWe report engineeringNeurospora crassato improve the yield of cellobiose and cellobionate from cellulose. A previously engineered strain ofN. crassa(F5) with six of seven β-glucosidase (bgl) genes knocked out was shown to produce cellobiose and cellobionate directly from cellulose without the addition of exogenous cellulases. In this study, the F5 strain was further modified to improve the yield of cellobiose and cellobionate from cellulose by increasing cellulase production and decreasing product consumption. The effects of two catabolite repression genes,cre-1andace-1, on cellulase production were investigated. The F5 Δace-1mutant showed no improvement over the wild type. The F5 Δcre-1and F5 Δace-1Δcre-1strains showed improved cellobiose dehydrogenase and exoglucanase expression. However, this improvement in cellulase expression did not lead to an improvement in cellobiose or cellobionate production. The cellobionate phosphorylase gene (ndvB) was deleted from the genome of F5 Δace-1Δcre-1to prevent the consumption of cellobiose and cellobionate. Despite a slightly reduced hydrolysis rate, the F5 Δace-1Δcre-1ΔndvBstrain converted 75% of the cellulose consumed to the desired products, cellobiose and cellobionate, compared to 18% converted by the strain F5 Δace-1Δcre-1.

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31

Guedon, E., S. Payot, M. Desvaux, and H. Petitdemange. "Carbon and Electron Flow in Clostridium cellulolyticum Grown in Chemostat Culture on Synthetic Medium." Journal of Bacteriology 181, no. 10 (1999): 3262–69. http://dx.doi.org/10.1128/jb.181.10.3262-3269.1999.

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ABSTRACT Previous results indicated poor sugar consumption and early inhibition of metabolism and growth when Clostridium cellulolyticum was cultured on medium containing cellobiose and yeast extract. Changing from complex medium to a synthetic medium had a strong effect on (i) the specific cellobiose consumption, which was increased threefold; and (ii) the electron flow, since the NADH/NAD+ ratios ranged from 0.29 to 2.08 on synthetic medium whereas ratios as high as 42 to 57 on complex medium were observed. These data indicate a better control of the carbon flow on mineral salts medium than on complex medium. By continuous culture, it was shown that the electron flow from glycolysis was balanced by the production of hydrogen gas, ethanol, and lactate. At low levels of carbon flow, pyruvate was preferentially cleaved to acetate and ethanol, enabling the bacteria to maximize ATP formation. A high catabolic rate led to pyruvate overflow and to increased ethanol and lactate production. In vitro, glyceraldehyde-3-phosphate dehydrogenase, lactate dehydrogenase, and ethanol dehydrogenase levels were higher under conditions giving higher in vivo specific production rates. Redox balance is essentially maintained by NADH-ferredoxin reductase-hydrogenase at low levels of carbon flow and by ethanol dehydrogenase and lactate dehydrogenase at high levels of carbon flow. The same maximum growth rate (0.150 h−1) was found in both mineral salts and complex media, proving that the uptake of nutrients or the generation of biosynthetic precursors occurred faster than their utilization. On synthetic medium, cellobiose carbon was converted into cell mass and catabolized to produce ATP, while on complex medium, it served mainly as an energy supply and, if present in excess, led to an accumulation of intracellular metabolites as demonstrated for NADH. Cells grown on synthetic medium and at high levels of carbon flow were able to induce regulatory responses such as the production of ethanol and lactate dehydrogenase.

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32

Hallberg, B. Martin, Gunnar Henriksson, Göran Pettersson, Andrea Vasella, and Christina Divne. "Mechanism of the Reductive Half-reaction in Cellobiose Dehydrogenase." Journal of Biological Chemistry 278, no. 9 (2002): 7160–66. http://dx.doi.org/10.1074/jbc.m210961200.

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33

Ludwig, R., and D. Haltrich. "Cellobiose dehydrogenase production by Sclerotium species pathogenic to plants." Letters in Applied Microbiology 35, no. 3 (2002): 261–66. http://dx.doi.org/10.1046/j.1472-765x.2002.01170.x.

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34

Stoica, Leonard, Annika Lindgren-Sjölander, Tautgirdas Ruzgas, and Lo Gorton. "Biosensor Based on Cellobiose Dehydrogenase for Detection of Catecholamines." Analytical Chemistry 76, no. 16 (2004): 4690–96. http://dx.doi.org/10.1021/ac049582j.

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35

Hildebrand, Amanda, J. Bennett Addison, Takao Kasuga, and Zhiliang Fan. "Cellobionic acid inhibition of cellobiohydrolase I and cellobiose dehydrogenase." Biochemical Engineering Journal 109 (May 2016): 236–42. http://dx.doi.org/10.1016/j.bej.2016.01.024.

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36

Thallinger, Barbara, Martin Brandauer, Peter Burger, et al. "Cellobiose dehydrogenase functionalized urinary catheter as novel antibiofilm system." Journal of Biomedical Materials Research Part B: Applied Biomaterials 104, no. 7 (2015): 1448–56. http://dx.doi.org/10.1002/jbm.b.33491.

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37

Cohen, Jonathan D., Wenjun Bao, V. Renganathan, S. Sai Subramaniam, and Thomas M. Loehr. "Resonance Raman Spectroscopic Studies of Cellobiose Dehydrogenase fromPhanerochaete chrysosporium." Archives of Biochemistry and Biophysics 341, no. 2 (1997): 321–28. http://dx.doi.org/10.1006/abbi.1997.9987.

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38

Li, Bin, Frederik A. J. Rotsaert, Michael H. Gold, and V. Renganathan. "Homologous Expression of Recombinant Cellobiose Dehydrogenase in Phanerochaete chrysosporium." Biochemical and Biophysical Research Communications 270, no. 1 (2000): 141–46. http://dx.doi.org/10.1006/bbrc.2000.2381.

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39

Loose, Jennifer S. M., Zarah Forsberg, Daniel Kracher, et al. "Activation of bacterial lytic polysaccharide monooxygenases with cellobiose dehydrogenase." Protein Science 25, no. 12 (2016): 2175–86. http://dx.doi.org/10.1002/pro.3043.

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40

IGARASHI, Kiyohiko, Ikuo MOMOHARA, Takeshi NISHINO, and Masahiro SAMEJIMA. "Kinetics of inter-domain electron transfer in flavocytochrome cellobiose dehydrogenase from the white-rot fungus Phanerochaete chrysosporium." Biochemical Journal 365, no. 2 (2002): 521–26. http://dx.doi.org/10.1042/bj20011809.

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The pre-steady-state kinetics of inter-domain electron transfer in the extracellular flavocytochrome cellobiose dehydrogenase from Phanerochaete chrysosporium was studied using various values of pH and substrate concentration. Monitoring at the isosbestic point of each prosthetic group indicated that the reductive half-reactions of flavin and haem were biphasic and monophasic respectively. When the observed rates of the flavin and haem reactions were plotted against substrate concentration, the behaviour of the second phase of the flavin reduction was almost identical with that of haem reduction at all substrate concentrations and pH values tested, suggesting that the formation of flavin semiquinone and haem reduction involve the same electron transfer reaction. Although flavin reduction by cellobiose was observed in the range of pH3.0–7.0, the velocity of the next electron transfer step decreased with increase of pH and was almost zero above pH6.0. The second phase of flavin reduction and the haem reduction were inhibited similarly by high concentrations of the substrate, whereas the first phase of flavin reduction showed a hyperbolic relation to the cellobiose concentration. Increase in pH enhanced the substrate inhibition of haem reduction but not the initial flavin reduction. Moreover, the dissociation constant Kd of flavin reduction and the substrate inhibition constant Ki of haem reduction decreased similarly with an increase of pH. From these results, it is evident that binding of cellobiose to the active site inhibits electron transfer from flavin to haem.

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41

Lipovsky, Anat, Barbara Thallinger, Ilana Perelshtein, et al. "Ultrasound coating of polydimethylsiloxanes with antimicrobial enzymes." Journal of Materials Chemistry B 3, no. 35 (2015): 7014–19. http://dx.doi.org/10.1039/c5tb00671f.

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Enzyme cellobiose dehydrogenase (CDH) nanoparticles were created by the ultrasonic waves and subsequently deposited on the PDMS surface. PDMS sheets treated for 3 min significantly reduce the amount of viableS. aureuscells as well as the total amount of biomass deposited on the surface.

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42

Ryu, Seunghyun, Julie Hipp, and Cong T. Trinh. "Activating and Elucidating Metabolism of Complex Sugars in Yarrowia lipolytica." Applied and Environmental Microbiology 82, no. 4 (2015): 1334–45. http://dx.doi.org/10.1128/aem.03582-15.

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ABSTRACTThe oleaginous yeastYarrowia lipolyticais an industrially important host for production of organic acids, oleochemicals, lipids, and proteins with broad biotechnological applications. Albeit known for decades, the unique native metabolism ofY. lipolyticafor using complex fermentable sugars, which are abundant in lignocellulosic biomass, is poorly understood. In this study, we activated and elucidated the native sugar metabolism inY. lipolyticafor cell growth on xylose and cellobiose as well as their mixtures with glucose through comprehensive metabolic and transcriptomic analyses. We identified 7 putative glucose-specific transporters, 16 putative xylose-specific transporters, and 4 putative cellobiose-specific transporters that are transcriptionally upregulated for growth on respective single sugars.Y. lipolyticais capable of using xylose as a carbon source, but xylose dehydrogenase is the key bottleneck of xylose assimilation and is transcriptionally repressed by glucose.Y. lipolyticahas a set of 5 extracellular and 6 intracellular β-glucosidases and is capable of assimilating cellobiose via extra- and intracellular mechanisms, the latter being dominant for growth on cellobiose as a sole carbon source. Strikingly,Y. lipolyticaexhibited enhanced sugar utilization for growth in mixed sugars, with strong carbon catabolite activation for growth on the mixture of xylose and cellobiose and with mild carbon catabolite repression of glucose on xylose and cellobiose. The results of this study shed light on fundamental understanding of the complex native sugar metabolism ofY. lipolyticaand will help guide inverse metabolic engineering ofY. lipolyticafor enhanced conversion of biomass-derived fermentable sugars to chemicals and fuels.

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Cameron, Michael D., Zachary D. Post, James D. Stahl, Joachim Haselbach, and Steven D. Aust. "Cellobiose dehydrogenase-dependent biodegradation of polyacrylate polymers by Phanerochaete chrysosporium." Environmental Science and Pollution Research 7, no. 3 (2000): 130–34. http://dx.doi.org/10.1065/espr2000.04.022.

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Henriksson, Gunnar, Liming Zhang, Jiebing Li, et al. "Is cellobiose dehydrogenase from Phanerochaete chrysosporium a lignin degrading enzyme?" Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1480, no. 1-2 (2000): 83–91. http://dx.doi.org/10.1016/s0167-4838(00)00096-0.

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Subramaniam, Sai S., Srinivasa R. Nagalla, and V. Renganathan. "Cloning and Characterization of a Thermostable Cellobiose Dehydrogenase fromSporotrichum thermophile." Archives of Biochemistry and Biophysics 365, no. 2 (1999): 223–30. http://dx.doi.org/10.1006/abbi.1999.1152.

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Saibi, Walid, та Ali Gargouri. "Cellobiose dehydrogenase influences the production of S. microspora β-glucosidase". World Journal of Microbiology and Biotechnology 28, № 1 (2011): 23–29. http://dx.doi.org/10.1007/s11274-011-0787-2.

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47

Igarashi, Kiyohiko, Masahiro Samejima, Yoshimasa Saburi, Naoto Habu, and Karl-Erik L. Eriksson. "Localization of Cellobiose Dehydrogenase in Cellulose-Grown Cultures ofPhanerochaete chrysosporium." Fungal Genetics and Biology 21, no. 2 (1997): 214–22. http://dx.doi.org/10.1006/fgbi.1996.0954.

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48

Baminger, Ursula, Sai S. Subramaniam, V. Renganathan, and Dietmar Haltrich. "Purification and Characterization of Cellobiose Dehydrogenase from the Plant Pathogen Sclerotium(Athelia) rolfsii." Applied and Environmental Microbiology 67, no. 4 (2001): 1766–74. http://dx.doi.org/10.1128/aem.67.4.1766-1774.2001.

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ABSTRACT 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), cytochromec, 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, β-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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Carrel, François L. Y., та Giorgio Canevascini. "Effect of β-glucosidase inhibitors on synthesis of cellulase and β-glucosidase in Sporotrichum (Chrysosporium) thermophile". Canadian Journal of Microbiology 37, № 6 (1991): 459–64. http://dx.doi.org/10.1139/m91-076.

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The addition of nojirimycin or gluconolactam, substances known as β-glucosidase inhibitors, to cultures of Sporotrichum (Chrysosporium) thermophile growing on cellobiose, caused a twofold or even higher increase (inhibited by cycloheximide) of the intracellular activity of this enzyme, but did not stimulate the synthesis of endocellulase or of cellobiose dehydrogenase. At concentrations from 0.1 to 1.0 mM, nojirimycin stimulated β-glucosidase synthesis to an extent apparently independent of concentration but did not affect cellular respiration on cellobiose. At 5 mM, however, cellobiose assimilation and subsequent growth were significantly but only temporarily impaired and β-glucosidase synthesis, which was still stimulated, was correspondingly delayed. Growth on glucose, on the other hand, was completely unaffected by nojirimycin. Upon fast protein liquid chromatography (FPLC) fractionation by gel filtration of mycelial extracts from cultures grown in the presence and in the absence of nojirimycin (0.1 mM), the β-glucosidase was recovered (67–70%) in two distinct fractions, A and B. The observed increase in β-glucosidase activity for cultures with nojirimycin was found to parallel the increase of fraction B. Key words: β-glucosidase inhibition, nojirimycin, cellulase biosynthesis.

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Raı́ces, Manuel, Raquel Montesino, José Cremata, et al. "Cellobiose quinone oxidoreductase from the white rot fungus Phanerochaete chrysosporium is produced by intracellular proteolysis of cellobiose dehydrogenase." Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression 1576, no. 1-2 (2002): 15–22. http://dx.doi.org/10.1016/s0167-4781(02)00243-9.

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