Evidence map›Paper›PMID 29075324›Full record

ArticleBiotechnology for biofuels2017

Comparative characterization of all cellulosomal cellulases from

Benedikt Leis, Claudia Held, Fabian Bergkemper, Katharina Dennemarck, Robert Steinbauer, Alarich Reiter, Matthias Mechelke, Matthias Moerch, Sigrid Graubner, Wolfgang Liebl and 2 more

Open access · goldAbstract read
In one paragraph

Article in Biotechnology for biofuels, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.8field-weighted citation impact, top 6% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

21 citing papers in PubMed, 57 citations in OpenAlex.

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  11. The Role ofMicroorganisms · 2020
    Article
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  13. EngineeringBiotechnology for biofuels · 2020
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors at 2 institutions in 2 countries.

Benedikt Leis *Department of Microbiology, Technische Universität München, Emil-Ramann-Str. 4, 85354 Freising, Germany.
Claudia Held *Department of Microbiology, Technische Universität München, Emil-Ramann-Str. 4, 85354 Freising, Germany.
Fabian BergkemperDepartment of Microbiology, Technische Universität München, Emil-Ramann-Str. 4, 85354 Freising, Germany.
Katharina DennemarckDepartment of Microbiology, Technische Universität München, Emil-Ramann-Str. 4, 85354 Freising, Germany.
Robert SteinbauerDepartment of Microbiology, Technische Universität München, Emil-Ramann-Str. 4, 85354 Freising, Germany.
Alarich ReiterDepartment of Microbiology, Technische Universität München, Emil-Ramann-Str. 4, 85354 Freising, Germany.
Matthias MechelkeDepartment of Microbiology, Technische Universität München, Emil-Ramann-Str. 4, 85354 Freising, Germany.
Matthias MoerchDepartment of Microbiology, Technische Universität München, Emil-Ramann-Str. 4, 85354 Freising, Germany.
Sigrid GraubnerDepartment of Microbiology, Technische Universität München, Emil-Ramann-Str. 4, 85354 Freising, Germany.
Wolfgang LieblDepartment of Microbiology, Technische Universität München, Emil-Ramann-Str. 4, 85354 Freising, Germany.
Wolfgang H SchwarzDepartment of Microbiology, Technische Universität München, Emil-Ramann-Str. 4, 85354 Freising, Germany.
Vladimir V ZverlovDepartment of Microbiology, Technische Universität München, Emil-Ramann-Str. 4, 85354 Freising, Germany.ORCID 0000-0002-0457-0284
Technical University of Munich · DEKurchatov Institute · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

background

resultsAlthough all 24 single-cellulosomal cellulases were described previously, we present the first comparative catalogue of all these enzymes together with a comprehensive analysis under identical experimental conditions, including enzyme activity, binding characteristics, substrate specificity, and product analysis. In the course of our study, we encountered four types of distinct enzymatic hydrolysis modes denoted by substrate specificity and hydrolysis product formation: (i) exo-mode cellobiohydrolases (CBH), (ii) endo-mode cellulases with no specific hydrolysis pattern, endoglucanases (EG), (iii) processive endoglucanases with cellotetraose as intermediate product (pEG4), and (iv) processive endoglucanases with cellobiose as the main product (pEG2). These modes are shown on amorphous cellulose and on model cello-oligosaccharides (with degree of polymerization DP 3 to 6). Artificial mini-cellulosomes carrying combinations of cellulases showed their highest activity when all four endoglucanase-groups were incorporated into a single complex. Such a modeled nonavalent complex (

conclusionsThe identification of a new endoglucanase type expands the list of known cellulase functions present in the cellulosome. Our study shows that the variety of processivities in the enzyme complex is a key enabler of its high cellulolytic efficiency. The observed synergistic effect may pave the way for a better understanding of the enzymatic interactions and the design of more active lignocellulose-degrading cellulase cocktails in the future.

Indexed as

Biomass degradationCellobiohydrolaseCellulaseCellulosomeEndoglucanaseMolecular dockingSynergistic hydrolysisSynthetic complex

Identifiers

PMID29075324
PMCPMC5651568
OpenAlexW2766367281

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.