Purified cellobiose dehydrogenase of Termitomyces sp. OE147 fuels cellulose degradation resulting in the release of reducing sugars

2020 ◽  
pp. 1-9
Author(s):  
Rishabh Gangwar ◽  
Shafaq Rasool ◽  
Saroj Mishra
Keyword(s):  
Reducing Sugars ◽  
Cellulose Degradation ◽  
Cellobiose Dehydrogenase

Endo-1, 4-β-glucanase and β-glucosidase of the ciliate Polyplastron multivesiculatum free of cellulolytic bacteria

1986 ◽  
Vol 32 (3) ◽  
pp. 219-225 ◽  
Author(s):  
A. Bonhomme ◽  
G. Fonty ◽  
M. J. Foglietti ◽  
D. Robic ◽  
M. Weber
Keyword(s):  
Enzymatic Activity ◽  
Isoelectric Focusing ◽  
Reducing Sugars ◽  
Proteolytic Enzymes ◽  
Cellulose Degradation ◽  
Protein Fractions ◽  
Intracellular Bacteria ◽  
Cellulolytic Bacteria ◽  
Derivatives Of ◽  
Bacterial Cellulase

To determine the contribution of protozoal activity to cellulose degradation, we maintained the ciliate Polyplastron multivesiculatum free of extracellular and intracellular cellulolytic bacteria. Control experiments to verify the absence of such bacteria were performed on cellular extracts, on filtrates, and on ciliates before lyophilization. The enzymatic activity was determined by viscometry and by determining the amount of reducing sugars produced. The enzyme was found to be an endo-1, 4- β-glucanase. Polyplastron multivesiculatum which was maintained free of extracellular and intracellular bacteria degraded soluble derivatives of cellulose and slightly degraded native cellulose. The activity was not due to intracellular bacterial cellulase, as ingested bacteria were lysed and digested by proteolytic enzymes of the protozoan. In addition, when preparing the filtrate solutions, P. multivesiculatum was maintained in culture for 5 days with Streptococcus faecalis (a facultatively anaerobic, noncellulolytic bacterium). Isoelectric focusing and chromatofocusing of lyophilized P. multivesiculatum that was free of cellulolytic bacteria yielded three protein fractions that degrade carboxymethylcellulose and hydroxyethylcellulose. Chromatofocusing also revealed the presence of two protein fractions with β-glucosidase activity.

scholarly journals Cellobiose dehydrogenase: An essential enzyme for lignocellulose degradation in nature – A review / Cellobiosedehydrogenase: Ein essentielles Enzym für den Lignozelluloseabbau in der Natur – Eine Übersicht

2016 ◽  
Vol 67 (3) ◽  
pp. 145-163 ◽  
Author(s):  
Daniel Kracher ◽  
Roland Ludwig
Keyword(s):  
Cellulose Degradation ◽  
Physiological Role ◽  
Cellobiose Dehydrogenase ◽  
Biofuel Production ◽  
Lignocellulose Degradation ◽  
Crystalline Cellulose ◽  
Biomass Processing ◽  
Essential Enzyme ◽  
Heme Cofactor

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.

Oxidative cellulose degradation by cellobiose dehydrogenase from Phanerochaete chrysosporium: A model compound study

Holzforschung ◽  
2005 ◽  
Vol 59 (3) ◽  
pp. 263-268 ◽  
Author(s):  
Martin Kruså ◽  
Gunnar Henriksson ◽  
Gunnar Johansson ◽  
Torbjörn Reitberger ◽  
Helena Lennholm
Keyword(s):  
Hydrogen Peroxide ◽  
Molecular Oxygen ◽  
Phanerochaete Chrysosporium ◽  
Hydroxyl Radicals ◽  
Gluconic Acid ◽  
Model Compound ◽  
Cellulose Degradation ◽  
Extracellular Enzyme ◽  
Cellobiose Dehydrogenase ◽  
Cellulose Depolymerization

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.

scholarly journals Phanerochaete chrysosporiumCellobiohydrolase and Cellobiose Dehydrogenase Transcripts in Wood

1998 ◽  
Vol 64 (5) ◽  
pp. 1924-1928 ◽  
Author(s):  
Marcelo A. Vallim ◽  
Bernard J. H. Janse ◽  
Jill Gaskell ◽  
Aline A. Pizzirani-Kleiner ◽  
Daniel Cullen
Keyword(s):  
Phanerochaete Chrysosporium ◽  
Cellulose Degradation ◽  
Cellobiose Dehydrogenase ◽  
Wood Chips ◽  
Defined Media

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.

scholarly journals Structural basis for cellobiose dehydrogenase action during oxidative cellulose degradation

2015 ◽  
Vol 6 (1) ◽  
Author(s):  
Tien-Chye Tan ◽  
Daniel Kracher ◽  
Rosaria Gandini ◽  
Christoph Sygmund ◽  
Roman Kittl ◽  
...  
Keyword(s):  
Cellulose Degradation ◽  
Cellobiose Dehydrogenase ◽  
Structural Basis

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
Keyword(s):  
Neurospora Crassa ◽  
Cellulose Degradation ◽  
Cellobiose Dehydrogenase ◽  
Polysaccharide Monooxygenase

QUALITATIVE AND QUANTITATIVE PHYTOCHEMICAL SCREENING AND IN VITRO ANTIOXIDANT EVALUATION OF PERGULARIA DAEMIA

2018 ◽  
Vol 24 (2) ◽  
Author(s):  
GITA MISHRA ◽  
HEMESHWER KUMAR CHANDRA ◽  
NISHA SAHU ◽  
SATENDRA KUMAR NIRALA ◽  
MONIKA BHADAURIA
Keyword(s):  
Reducing Sugars ◽  
Antioxidant Properties ◽  
Phytochemical Analysis ◽  
Phytochemical Screening ◽  
Qualitative And Quantitative ◽  
The Family ◽  
Ethanolic Extracts ◽  
Antioxidant Evaluation ◽  
In Vitro Antioxidant Activity

Pergularia daemia belongs to the family Asclepiadaceae, known to have anticancer, anti-inflammatory activity. Aim of the present study was to evaluate qualitative and quantitative phytochemical and antioxidant properties of ethanolic extracts of leaf, stem and root parts of P. daemia . Preliminary phytochemical analysis and in vitro antioxidant properties were evaluated by standard methods. The qualitative phytochemical analysis of P. daemia showed presence of flavonoids, tannins, alkaloid, phytosterol, carbohydrate, phenol, saponin, glycosides, terpenoids, steroids proteins and reducing sugars. Quantitative analysis showed polyphenol, flavonoid, flavonone, flavone and flavonol in P. daemia leaves, stem and root in considerable quantity. The in vitro antioxidant activity of P. daemia clearly demonstrated that leaf, stem and root parts have prominent antioxidant properties and was effective in scavenging free radicals.

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