Evidence map›Paper›PMID 28894250›Full record

ArticleScientific reports2017

Identification of endoxylanase XynE from Clostridium thermocellum as the first xylanase of glycoside hydrolase family GH141.

Simon Heinze, Matthias Mechelke, Petra Kornberger, Wolfgang Liebl, Wolfgang H Schwarz, Vladimir V Zverlov

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

14 citing papers in PubMed, 35 citations in OpenAlex.

  1. Whole-genome analysis and enzymatic profiling of Bacillus spizizenii as a xylanase-producing source from Iran.International microbiology : the official journal of the Spanish Society for Microbiology · 2026
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  2. Review
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  4. Recent progress in the microbial production of Xylanase.World journal of microbiology & biotechnology · 2025
    Review
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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

6 authors at 2 institutions in 2 countries.

Simon HeinzeDepartment of Microbiology, Technical University of Munich, Emil-Ramann-Str. 4, D-85354, Freising-Weihenstephan, Germany.ORCID 0000-0002-8518-4341
Matthias MechelkeDepartment of Microbiology, Technical University of Munich, Emil-Ramann-Str. 4, D-85354, Freising-Weihenstephan, Germany.ORCID 0000-0003-2011-4315
Petra KornbergerDepartment of Microbiology, Technical University of Munich, Emil-Ramann-Str. 4, D-85354, Freising-Weihenstephan, Germany.ORCID 0000-0002-5466-4174
Wolfgang LieblDepartment of Microbiology, Technical University of Munich, Emil-Ramann-Str. 4, D-85354, Freising-Weihenstephan, Germany. wliebl@wzw.tum.de.ORCID 0000-0002-8421-2478
Wolfgang H SchwarzDepartment of Microbiology, Technical University of Munich, Emil-Ramann-Str. 4, D-85354, Freising-Weihenstephan, Germany.ORCID 0000-0001-9290-8558
Vladimir V ZverlovDepartment of Microbiology, Technical University of Munich, Emil-Ramann-Str. 4, D-85354, Freising-Weihenstephan, Germany. vladimir.zverlov@tum.de.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

Enzymes that cleave polysaccharides in lignocellulose, i. e., cellulases, xylanases, and accessory enzymes, play crucial roles in the natural decomposition of plant-derived biomass and its efficient and sustainable processing into biofuels or other bulk chemicals. The analysis of open reading frame cthe_2195 from the thermophilic, cellulolytic anaerobe Clostridium thermocellum (also known as 'Ruminiclostridium thermocellum') suggested that it encoded a cellulosomal protein comprising a dockerin-I module, a carbohydrate-binding module, and a module of previously unknown function. The biochemical characterisation upon recombinant expression in Escherichia coli revealed that the protein is a thermostable endoxylanase, named Xyn141E with an optimal pH of 6.0-6.5 and a temperature optimum of 67-75 °C. The substrate spectrum of Xyn141E resembles that of GH10 xylanases, because of its side activities on carboxymethyl cellulose, barley β-glucan, and mannan. Conversely, the product spectrum of Xyn141E acting on arabinoxylan is similar to those of GH11, as established by HPAEC-PAD analysis. Xyn141E is weakly related (20.7% amino acid sequence identity) to the founding member of the recently established GH family 141 and is the first xylanase in this new family of biomass-degrading enzymes.

Indexed as

Acetivibrio thermocellusCloning, MolecularComputational BiologyEndo-1,4-beta XylanasesEnzyme StabilityEscherichia coliGene ExpressionHydrogen-Ion ConcentrationPolysaccharidesProtein DomainsRecombinant ProteinsSubstrate SpecificityTemperatureEndo-1,4-beta XylanasesPolysaccharidesRecombinant Proteins

Identifiers

PMID28894250
PMCPMC5593877
OpenAlexW2752975460

What OpenQuestion holds

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Registered trials

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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.