Evidence map›Paper›PMID 26741138›Full record

ArticlePloS one2016

Discovery and Characterization of a Thermostable and Highly Halotolerant GH5 Cellulase from an Icelandic Hot Spring Isolate.

Dimitra Zarafeta, Dimitrios Kissas, Christopher Sayer, Sóley R Gudbergsdottir, Efthymios Ladoukakis, Michail N Isupov, Aristotelis Chatziioannou, Xu Peng, Jennifer A Littlechild, Georgios Skretas and 1 more

Abstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
–field-weighted citation impact
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

26 citing papers in PubMed.

  1. Article
  2. Article
  3. Biomimetic COEnvironmental science & technology · 2024
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Isolation of3 Biotech · 2022
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. XynDZ5: A New Thermostable GH10 Xylanase.Frontiers in microbiology · 2020
    Article
  18. Article
  19. Review
  20. 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

11 authors.

Dimitra ZarafetaInstitute of Biology, Medicinal Chemistry & Biotechnology, National Hellenic Research Foundation, Athens, Greece.
Dimitrios KissasInstitute of Biology, Medicinal Chemistry & Biotechnology, National Hellenic Research Foundation, Athens, Greece.
Christopher SayerHenry Wellcome Building for Biocatalysis, Biosciences, College of Life and Environmental Sciences, University of Exeter, Exeter, United Kingdom.
Sóley R GudbergsdottirDanish Archaea Centre, Department of Biology, Copenhagen University, Copenhagen, Denmark.
Efthymios LadoukakisLaboratory of Biotechnology, School of Chemical Engineering, National Technical University of Athens, Athens, Greece.
Michail N IsupovHenry Wellcome Building for Biocatalysis, Biosciences, College of Life and Environmental Sciences, University of Exeter, Exeter, United Kingdom.
Aristotelis ChatziioannouInstitute of Biology, Medicinal Chemistry & Biotechnology, National Hellenic Research Foundation, Athens, Greece.
Xu PengDanish Archaea Centre, Department of Biology, Copenhagen University, Copenhagen, Denmark.
Jennifer A LittlechildHenry Wellcome Building for Biocatalysis, Biosciences, College of Life and Environmental Sciences, University of Exeter, Exeter, United Kingdom.
Georgios SkretasInstitute of Biology, Medicinal Chemistry & Biotechnology, National Hellenic Research Foundation, Athens, Greece.
Fragiskos N KolisisLaboratory of Biotechnology, School of Chemical Engineering, National Technical University of Athens, Athens, Greece.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

With the ultimate goal of identifying robust cellulases for industrial biocatalytic conversions, we have isolated and characterized a new thermostable and very halotolerant GH5 cellulase. This new enzyme, termed CelDZ1, was identified by bioinformatic analysis from the genome of a polysaccharide-enrichment culture isolate, initiated from material collected from an Icelandic hot spring. Biochemical characterization of CelDZ1 revealed that it is a glycoside hydrolase with optimal activity at 70°C and pH 5.0 that exhibits good thermostability, high halotolerance at near-saturating salt concentrations, and resistance towards metal ions and other denaturing agents. X-ray crystallography of the new enzyme showed that CelDZ1 is the first reported cellulase structure that lacks the defined sugar-binding 2 subsite and revealed structural features which provide potential explanations of its biochemical characteristics.

Indexed as

Bacterial ProteinsCatalytic DomainCellulaseCelluloseChloridesCrystallography, X-RayEnzyme StabilityHot SpringsHot TemperatureHydrogen-Ion ConcentrationIcelandKineticsModels, MolecularSalt ToleranceSubstrate SpecificityThermoanaerobacterBacterial ProteinsCellulaseCelluloseChlorides

Identifiers

PMID26741138
PMCPMC4704807

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.