Evidence map›Paper›PMID 32308737›Full record

ArticleBiotechnology for biofuels2020

Investigation of a thermostable multi-domain xylanase-glucuronoyl esterase enzyme from

Daniel Krska, Johan Larsbrink

Open access · goldAbstract read
In one paragraph

Article in Biotechnology for biofuels, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

16 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
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  6. Review
  7. Thermostable enzyme research advances: a bibliometric analysis.Journal, genetic engineering & biotechnology · 2023
    Review
  8. Article
  9. Article
  10. Understanding the Role ofAnimals : an open access journal from MDPI · 2021
    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

2 authors at 1 institution in 1 country.

Daniel Krska1Division of Industrial Biotechnology, Department of Biology and Biological Engineering, Chalmers University of Technology, 412 96 Gothenburg, Sweden.
Johan Larsbrink1Division of Industrial Biotechnology, Department of Biology and Biological Engineering, Chalmers University of Technology, 412 96 Gothenburg, Sweden.ORCID 0000-0001-8386-2914
Chalmers University of Technology · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundEfficient degradation of lignocellulosic biomass has become a major bottleneck in industrial processes which attempt to use biomass as a carbon source for the production of biofuels and materials. To make the most effective use of the source material, both the hemicellulosic as well as cellulosic parts of the biomass should be targeted, and as such both hemicellulases and cellulases are important enzymes in biorefinery processes. Using thermostable versions of these enzymes can also prove beneficial in biomass degradation, as they can be expected to act faster than mesophilic enzymes and the process can also be improved by lower viscosities at higher temperatures, as well as prevent the introduction of microbial contamination.

resultsThis study presents the investigation of the thermostable, dual-function xylanase-glucuronoyl esterase enzyme

conclusionsDue to its thermostability,

Indexed as

BiomassCaldicellulosiruptor kristjansoniiCarbohydrate-active enzymeCarbohydrate-binding moduleGlucuronoyl esteraseLignin–carbohydrate complexesThermostabilityXylanXylanase

Identifiers

PMID32308737
PMCPMC7151638
OpenAlexW3016870548

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.