ArticleMicrobial cell factories2017
Molecular and catalytic properties of fungal extracellular cellobiose dehydrogenase produced in prokaryotic and eukaryotic expression systems.
Article in Microbial cell factories, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
15 citing papers in PubMed, 48 citations in OpenAlex.
- High-efficiency secretion expression of FAD-dependent glucose dehydrogenase in Pichia pastoris via signal peptide optimization and redox cofactor enhancement.Bioprocess and biosystems engineering · 2026Article
- Current Understanding on the Heterogenous Expression of Plastic Depolymerising Enzymes inBioengineering (Basel, Switzerland) · 2025Review
- Exploring class III cellobiose dehydrogenase: sequence analysis and optimized recombinant expression.Microbial cell factories · 2024Article
- Expression of cellobiose dehydrogenase gene inFrontiers in microbiology · 2024Article
- Heterologous protein production in filamentous fungi.Applied microbiology and biotechnology · 2023Review
- Interdomain Linker of the Bioelecrocatalyst Cellobiose Dehydrogenase Governs the Electron Transfer.ACS catalysis · 2023Article
- Insights into plastic biodegradation: community composition and functional capabilities of the superworm (Microbial genomics · 2022Article
- Article
- Efficient Constitutive Expression of Cellulolytic Enzymes inJournal of microbiology and biotechnology · 2021Article
- Microbial Interkingdom Biofilms and the Quest for Novel Therapeutic Strategies.Microorganisms · 2021Review
- Heterologous expression of Phanerochaete chrysosporium cellobiose dehydrogenase in Trichoderma reesei.Microbial cell factories · 2021Article
- Article
- Scalable methanol-free production of recombinant glucuronoyl esterase in Pichia pastoris.BMC research notes · 2019Article
- Direct Electron Transfer of Enzymes Facilitated by Cytochromes.ChemElectroChem · 2019Review
- The Promoter Toolbox for Recombinant Gene Expression inFrontiers in bioengineering and biotechnology · 2018Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 5 institutions in 4 countries.
Funding
Abstract
backgroundCellobiose dehydrogenase (CDH) is an extracellular enzyme produced by lignocellulolytic fungi. cdh gene expression is high in cellulose containing media, but relatively low CDH concentrations are found in the supernatant of fungal cultures due to strong binding to cellulose. Therefore, heterologous expression of CDH in Pichia pastoris was employed in the last 15 years, but the obtained enzymes were over glycosylated and had a reduced specific activity.
resultsWe compare the well-established CDH expression host P. pastoris with the less frequently used hosts Escherichia coli, Aspergillus niger, and Trichoderma reesei. The study evaluates the produced quantity and protein homogeneity of Corynascus thermophilus CDH in the culture supernatants, the purification, and finally compares the enzymes in regard to cofactor loading, glycosylation, catalytic constants and thermostability.
conclusionsWhereas E. coli could only express the catalytic dehydrogenase domain of CDH, all eukaryotic hosts could express full length CDH including the cytochrome domain. The CDH produced by T. reesei was most similar to the CDH originally isolated from the fungus C. thermophilus in regard to glycosylation, cofactor loading and catalytic constants. Under the tested experimental conditions the fungal expression hosts produce CDH of superior quality and uniformity compared to P. pastoris.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.