Evidence map›Paper›PMID 32390953›Full record

ArticleFrontiers in microbiology2020

XynDZ5: A New Thermostable GH10 Xylanase.

Dimitra Zarafeta, Anastasia P Galanopoulou, Maria Evangelia Leni, Stavroula I Kaili, Magda S Chegkazi, Evangelia D Chrysina, Fragiskos N Kolisis, Dimitris G Hatzinikolaou, Georgios Skretas

Open access · goldAbstract read
In one paragraph

Article in Frontiers in microbiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed, 32 citations in OpenAlex.

  1. Endo-β-1,4-Xylanase GH10 fromInternational journal of molecular sciences · 2026
    Article
  2. 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
    Article
  3. Article
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  6. Discovery andACS omega · 2025
    Article
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  8. Lignocellulolytic extremozymes and their biotechnological applications.Extremophiles : life under extreme conditions · 2023
    Review
  9. Article
  10. Article
  11. A thermostable and CBM2-linked GH10 xylanase fromFrontiers in bioengineering and biotechnology · 2022
    Article
  12. Frontiers in microbiology · 2022
    Article
  13. Article
  14. Article
  15. Review
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  17. Frontiers in microbiology · 2020
    Article
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

9 authors at 3 institutions in 1 country.

Dimitra ZarafetaInstitute of Chemical Biology, National Hellenic Research Foundation, Athens, Greece.
Anastasia P GalanopoulouInstitute of Chemical Biology, National Hellenic Research Foundation, Athens, Greece.
Maria Evangelia LeniInstitute of Chemical Biology, National Hellenic Research Foundation, Athens, Greece.
Stavroula I KailiDepartment of Biology, Enzyme and Microbial Biotechnology Unit, National and Kapodistrian University of Athens, Athens, Greece.
Magda S ChegkaziInstitute of Chemical Biology, National Hellenic Research Foundation, Athens, Greece.
Evangelia D ChrysinaInstitute of Chemical Biology, National Hellenic Research Foundation, Athens, Greece.
Fragiskos N KolisisLaboratory of Biotechnology, School of Chemical Engineering, National Technical University of Athens, Athens, Greece.
Dimitris G HatzinikolaouDepartment of Biology, Enzyme and Microbial Biotechnology Unit, National and Kapodistrian University of Athens, Athens, Greece.
Georgios SkretasInstitute of Chemical Biology, National Hellenic Research Foundation, Athens, Greece.
National Hellenic Research Foundation · GRNational and Kapodistrian University of Athens · GRNational Technical University of Athens · GR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Xylanolytic enzymes have a broad range of applications in industrial biotechnology as biocatalytic components of various processes and products, such as food additives, bakery products, coffee extraction, agricultural silage and functional foods. An increasing market demand has driven the growing interest for the discovery of xylanases with specific industrially relevant characteristics, such as stability at elevated temperatures and in the presence of other denaturing factors, which will facilitate their incorporation into industrial processes. In this work, we report the discovery and biochemical characterization of a new thermostable GH10 xylanase, termed XynDZ5, exhibiting only 26% amino acid sequence identity to the closest characterized xylanolytic enzyme. This new enzyme was discovered in an Icelandic hot spring enrichment culture of a

Indexed as

biocatalysisbiotechnologygenome analysismode of actionthermostabilityxylanase

Identifiers

PMID32390953
PMCPMC7193231
OpenAlexW3017589998

What OpenQuestion holds

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LicenceCC BY
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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.