Cellobiose dehydrogenase in biofuel cells

Scheiblbrandner, Stefan; Csarman, Florian; Ludwig, Roland

doi:10.1016/j.copbio.2021.08.013

Cited by 16 publications

(11 citation statements)

References 56 publications

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“…The field of bioelectrocatalysis at the ITIES is still in its infancy. Thus, studies with proteins beyond the model Cyt c system, such as oxidases [83] and dehydrogenases [84], are required to clarify the limitations and advantages of this new research topic. Furthermore, major scope exists to modify the liquidjliquid interface with phospholipid monolayers to enhance the biocompatibility of the ITIES and optimise IET with proteins.…”

Section: Discussionmentioning

confidence: 99%

Electrocatalysis at the polarised interface between two immiscible electrolyte solutions

Gamero‐Quijano

Herzog

Peljo

et al. 2023

Current Opinion in Electrochemistry

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Section: Discussionmentioning

confidence: 99%

Electrocatalysis at the polarised interface between two immiscible electrolyte solutions

Gamero‐Quijano

Herzog

Peljo

et al. 2023

Current Opinion in Electrochemistry

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“…Since CDH plays a pivotal role in oxidative degradation of recalcitrant polysaccharides and has great application potentials in biosensors and enzymatic biofuel cells, improving CDH properties by protein engineering had attracted the interest of many scientists. Current works included the engineering of CDH for improving its oxidizing activity, turnover or peroxide stability, and H 2 O 2 generation ability .…”

Section: Discussionmentioning

confidence: 99%

Unique Lysine-Rich Sequence on the CYT Domain of AfCDH Enhances Its Interdomain Electron Transfer and Activation of AA9 LPMOs

Chen

Yang

Ding

et al. 2022

ACS Sustainable Chem. Eng.

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Cellobiose dehydrogenase (CDH) is a biologically relevant electron donor for lytic polysaccharide monooxygenase (LPMO) in the oxidative cleavage of recalcitrant polysaccharides, so exploring the intrinsic factors affecting the electron transfer from CDH to LPMO is vital for governing the CDH-driven LPMO reaction efficiency. We previously found a unique lysine-rich sequence on the cytochrome (CYT) domain of Af CDH from Aspergillus fumigatus. Here, we comprehensively compared the functionality of Af CDH and Af CDHΔ (the lysine-rich sequencedeleted mutant) to elucidate the role and significance of the lysinerich sequence in its interdomain electron transfer (IDET) and activation of LPMOs. The results showed that the lysine-rich sequence had no influence on the dehydrogenase (DH) reductive half-reaction and the interprotein electron transfer (IPET) rate from CYT to LPMOs. However, a remarkably faster IDET rate between DH and CYT was observed in Af CDH compared to that in Af CDHΔ, especially under high pH conditions. Moreover, Af CDH was found to be more effective in driving the LPMO reactions than Af CDHΔ. Our findings demonstrated that IDET is crucial for the overall electron transfer from CDH to LPMO and the CDHdriven LPMO reaction efficiency. This work provides a feasible strategy for engineering the lysine-rich sequence on CYT to potentiate the IDET rate in other CDHs and for the activation of LPMO.

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“…The first CDH (belonging to class I) was identified in 1974 in the secretome of the white-rot fungus Phanerochaete chrysoporium [ 7 ]. Since then, a number of studies investigated the catalytic and biochemical properties of CDHs, as well as their potential applications [ 8 ], including the development of biosensors for the detection of carbohydrates, such as lactose [ 9 ] or glucose [ 10 ], andthe production of biofuel cells [ 11 ]. CDH mainly exhibits a two-domain structure consisting of a heme b -containing N-terminal cytochrome (Cyt) domain and a catalytic FAD-dependent dehydrogenase (DH) domain belonging to the glucose-methanol-choline (GMC) superfamily [ 6 , 12 – 14 ].…”

Section: Introductionmentioning

confidence: 99%

Exploring class III cellobiose dehydrogenase: sequence analysis and optimized recombinant expression

Giorgianni,

Zenone,

Sützl

et al. 2024

Microb Cell Fact

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Background Cellobiose dehydrogenase (CDH) is an extracellular fungal oxidoreductase with multiple functions in plant biomass degradation. Its primary function as an auxiliary enzyme of lytic polysaccharide monooxygenase (LPMO) facilitates the efficient depolymerization of cellulose, hemicelluloses and other carbohydrate-based polymers. The synergistic action of CDH and LPMO that supports biomass-degrading hydrolases holds significant promise to harness renewable resources for the production of biofuels, chemicals, and modified materials in an environmentally sustainable manner. While previous phylogenetic analyses have identified four distinct classes of CDHs, only class I and II have been biochemically characterized so far. Results Following a comprehensive database search aimed at identifying CDH sequences belonging to the so far uncharacterized class III for subsequent expression and biochemical characterization, we have curated an extensive compilation of putative CDH amino acid sequences. A sequence similarity network analysis was used to cluster them into the four distinct CDH classes. A total of 1237 sequences encoding putative class III CDHs were extracted from the network and used for phylogenetic analyses. The obtained phylogenetic tree was used to guide the selection of 11 cdhIII genes for recombinant expression in Komagataella phaffii. A small-scale expression screening procedure identified a promising cdhIII gene originating from the plant pathogen Fusarium solani (FsCDH), which was selected for expression optimization by signal peptide shuffling and subsequent production in a 5-L bioreactor. The purified FsCDH exhibits a UV-Vis spectrum and enzymatic activity similar to other characterized CDH classes. Conclusion The successful production and functional characterization of FsCDH proved that class III CDHs are catalytical active enzymes resembling the key properties of class I and class II CDHs. A detailed biochemical characterization based on the established expression and purification strategy can provide new insights into the evolutionary process shaping CDHs and leading to their differentiation into the four distinct classes. The findings have the potential to broaden our understanding of the biocatalytic application of CDH and LPMO for the oxidative depolymerization of polysaccharides.

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Cellobiose dehydrogenase in biofuel cells

Cited by 16 publications

References 56 publications

Electrocatalysis at the polarised interface between two immiscible electrolyte solutions

Electrocatalysis at the polarised interface between two immiscible electrolyte solutions

Unique Lysine-Rich Sequence on the CYT Domain of AfCDH Enhances Its Interdomain Electron Transfer and Activation of AA9 LPMOs

Exploring class III cellobiose dehydrogenase: sequence analysis and optimized recombinant expression

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