Evidence map›Paper›PMID 16532363›Full record

ArticleExtremophiles : life under extreme conditions2006

Cloning and characterization of a cold-active xylanase enzyme from an environmental DNA library.

Charles C Lee, Rena E Kibblewhite-Accinelli, Kurt Wagschal, George H Robertson, Dominic W S Wong

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Article in Extremophiles : life under extreme conditions, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Article
  2. Molecular and Biochemical Characterization of Xylanase Produced byJournal of microbiology and biotechnology · 2024
    Article
  3. Review
  4. Review
  5. Article
  6. Characterization of a novel cold-active xylanase from Luteimonas species.World journal of microbiology & biotechnology · 2018
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Alkaliphilic bacteria: applications in industrial biotechnology.Journal of industrial microbiology & biotechnology · 2011
    Review
  18. Article
  19. Crystallization and preliminary X-ray analysis of a cold-active endo-β-1,4-D-xylanase from glycoside hydrolase family 8.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011
    Article
  20. Article
4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

5 authors.

Charles C LeeUSDA-ARS-WRRC, 800 Buchanan St., Albany, CA 94710, USA. clee@pw.usda.gov
Rena E Kibblewhite-Accinelli
Kurt Wagschal
George H Robertson
Dominic W S Wong

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

There is a great interest in xylanases due to the wide variety of industrial applications for these enzymes. We cloned a xylanase gene (xyn8) from an environmental genomic DNA library. The encoded enzyme was predicted to be 399 amino acids with a molecular weight of 45.9 kD. The enzyme was categorized as a glycosyl hydrolase family 8 member based on sequence analysis of the putative catalytic domain. The purified enzyme was thermolabile, had an activity temperature optimum of 20 degrees C on native xylan substrate, and retained significant activity at lower temperatures. At 4 degrees C, the apparent K (m) was 3.7 mg/ml, and the apparent k (cat) was 123/s.

Indexed as

Gene LibraryWater MicrobiologyAgricultureAmino Acid SequenceBacterial ProteinsCaliforniaCloning, MolecularEnzyme StabilityHydrogen-Ion ConcentrationMolecular Sequence DataTemperatureXylosidasesBacterial ProteinsXylosidases

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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.