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

Kracher, Daniel; Ludwig, Roland

doi:10.1515/boku-2016-0013

Cited by 34 publications

(26 citation statements)

References 125 publications

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“…Today, there is strong evidence that CDH constitutes a natural redox partner for AA9 LPMOs (55,124,125) although the exact mode of interplay still needs to be fully elucidated, including the second-electron conundrum in the O 2 -based LPMO mechanism. Considering the recent doubts concerning this mechanism, it is worthwhile to revisit some of the available kinetic data for CDHs and their interplay with LPMOs.…”

Section: The Cdh Case: a Multifunctional Redox Partner?mentioning

confidence: 99%

“…It is known that the reduced Cyt domain can transfer electrons to AA9 and AA10 LPMOs (102,124). The existence of a CDH binding site on a fungal AA9 LPMO has been suggested (127), but theoretical considerations (42) and lack of sequence conservation in the proposed docking site (125), as well as studies of interactions between CDH and an AA9 LPMO by computational modeling (124) or nuclear magnetic resonance (NMR) (55), rather support direct electron transfer at the copper site.…”

Section: The Cdh Case: a Multifunctional Redox Partner?mentioning

confidence: 99%

“…Comparing the high reduction rate of the FAD domain (by electrons derived from oligosaccharide oxidation) with all other rates of subsequent reactions in the CDH system ( Fig. 5) shows that the rate of reoxidation of CDH is determining the overall turnover rate and that this rate is driven by the nature of the electron acceptor and its ability to accept electrons from CDH (Table S1) (125). In the CDH-LPMO systems, there is a mismatch between the (relatively high) electron-donating capacity of CDH and the (relatively low) electron consumption by the LPMO.…”

Section: The Cdh Case: a Multifunctional Redox Partner?mentioning

confidence: 99%

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Oxidoreductases and Reactive Oxygen Species in Conversion of Lignocellulosic Biomass

Bissaro

Várnai

Røhr

et al. 2018

Microbiol Mol Biol Rev

230

246

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SUMMARYBiomass constitutes an appealing alternative to fossil resources for the production of materials and energy. The abundance and attractiveness of vegetal biomass come along with challenges pertaining to the intricacy of its structure, evolved during billions of years to face and resist abiotic and biotic attacks. To achieve the daunting goal of plant cell wall decomposition, microorganisms have developed many (enzymatic) strategies, from which we seek inspiration to develop biotechnological processes. A major breakthrough in the field has been the discovery of enzymes today known as lytic polysaccharide monooxygenases (LPMOs), which, by catalyzing the oxidative cleavage of recalcitrant polysaccharides, allow canonical hydrolytic enzymes to depolymerize the biomass more efficiently. Very recently, it has been shown that LPMOs are not classical monooxygenases in that they can also use hydrogen peroxide (H2O2) as an oxidant. This discovery calls for a revision of our understanding of how lignocellulolytic enzymes are connected since H2O2is produced and used by several of them. The first part of this review is dedicated to the LPMO paradigm, describing knowns, unknowns, and uncertainties. We then present different lignocellulolytic redox systems, enzymatic or not, that depend on fluxes of reactive oxygen species (ROS). Based on an assessment of these putatively interconnected systems, we suggest that fine-tuning of H2O2levels and proximity between sites of H2O2production and consumption are important for fungal biomass conversion. In the last part of this review, we discuss how our evolving understanding of redox processes involved in biomass depolymerization may translate into industrial applications.

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Section: The Cdh Case: a Multifunctional Redox Partner?mentioning

confidence: 99%

Section: The Cdh Case: a Multifunctional Redox Partner?mentioning

confidence: 99%

Section: The Cdh Case: a Multifunctional Redox Partner?mentioning

confidence: 99%

See 1 more Smart Citation

Oxidoreductases and Reactive Oxygen Species in Conversion of Lignocellulosic Biomass

Bissaro

Várnai

Røhr

et al. 2018

Microbiol Mol Biol Rev

230

246

View full text Add to dashboard Cite

show abstract

“…Only one crystal structure is available for the whole enzyme, extracted from Neurospora crassa and published by the same group recently [ 106 ]. The natural electron acceptor to CDH, lytic polysaccharide monooxygenase (LPMO) was only recently discovered [ 107 ] revealing the central role of CDH in the degradation of lignocellulose in nature [ 108 , 109 ].…”

Section: Cellobiose Dehydrogenasementioning

confidence: 99%

Direct Electron Transfer of Dehydrogenases for Development of 3rd Generation Biosensors and Enzymatic Fuel Cells

Bollella

Gorton

Antiochia

2018

Sensors

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Dehydrogenase based bioelectrocatalysis has been increasingly exploited in recent years in order to develop new bioelectrochemical devices, such as biosensors and biofuel cells, with improved performances. In some cases, dehydrogeases are able to directly exchange electrons with an appropriately designed electrode surface, without the need for an added redox mediator, allowing bioelectrocatalysis based on a direct electron transfer process. In this review we briefly describe the electron transfer mechanism of dehydrogenase enzymes and some of the characteristics required for bioelectrocatalysis reactions via a direct electron transfer mechanism. Special attention is given to cellobiose dehydrogenase and fructose dehydrogenase, which showed efficient direct electron transfer reactions. An overview of the most recent biosensors and biofuel cells based on the two dehydrogenases will be presented. The various strategies to prepare modified electrodes in order to improve the electron transfer properties of the device will be carefully investigated and all analytical parameters will be presented, discussed and compared.

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“…CDH finds application in multiple areas including bioremediation, textile, biomedicine, biosensors and biofuels [15]. CDH could improve the saccharification of pre-treated lignocellulose through reduction of end-product inhibition and catalytic activation of lytic polysaccharide monooxygenase [16]. This type of studies is necessary to facilitate research of the functionality and application of GE and other emerging enzymes such as CDH.…”

Section: Introductionmentioning

confidence: 99%

Scalable methanol-free production of recombinant glucuronoyl esterase in Pichia pastoris

et al. 2019

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Objective Glucuronoyl esterase (GE) is an emerging enzyme that improves fractionation of lignin-carbohydrate complexes. However, the commercial availability of GE is limited, which hinders the research of GE-based bioprocesses for its industrial application in lignocellulose biorefineries. This study evaluated a workable, cost-effective, and commercially scalable production strategy to improve the ease of GE-based research. This strategy consisted of a constitutive and methanol-free enzyme production step coupled with a two-step filtration process. The aim was to determine if this strategy can yield copious amounts of GE, by secretion into the extracellular medium with an acceptable purity that could allow its direct application. This approach was further validated for cellobiose dehydrogenase, another emerging lignocellulose degrading enzyme which is scarcely available at high cost. Results The secreted recombinant enzymes were functionally produced in excess of levels previously reported for constitutive production (1489–2780 mg L−1), and were secreted at moderate to high percentages of the total extracellular protein (51–94%). The constant glycerol feed, implemented during fed-batch fermentation, lead to a decline in growth rate and plateaued productivity. Tangential flow ultrafiltration was used to concentrate cell-free enzyme extracts 5–6-fold, reaching enzyme activity levels (1020–202 U L−1) that could allow their direct application.

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

Cited by 34 publications

References 125 publications

Oxidoreductases and Reactive Oxygen Species in Conversion of Lignocellulosic Biomass

Oxidoreductases and Reactive Oxygen Species in Conversion of Lignocellulosic Biomass

Direct Electron Transfer of Dehydrogenases for Development of 3rd Generation Biosensors and Enzymatic Fuel Cells

Scalable methanol-free production of recombinant glucuronoyl esterase in Pichia pastoris

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