Evidence map›Paper›PMID 32905355›Full record

ReviewBiotechnology for biofuels2020

Biomass-degrading glycoside hydrolases of archaeal origin.

Marcel Suleiman, Anna Krüger, Garabed Antranikian

Open access · goldAbstract readReview
In one paragraph

Review 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 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.4field-weighted citation impact, top 11% 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, 45 citations in OpenAlex.

  1. Article
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  5. Review
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  9. Article
  10. The Diversity, Composition, and Metabolic Pathways of Archaea in Pigs.Animals : an open access journal from MDPI · 2021
    Article
  11. Review
  12. Article
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  14. 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

3 authors at 1 institution in 2 countries.

Marcel SuleimanInstitute of Technical Microbiology, University of Technology Hamburg, Hamburg, Germany.
Anna KrügerInstitute of Technical Microbiology, University of Technology Hamburg, Hamburg, Germany.
Garabed AntranikianInstitute of Technical Microbiology, University of Technology Hamburg, Hamburg, Germany.
Hamburg University of Technology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

During the last decades, the impact of hyperthermophiles and their enzymes has been intensively investigated for implementation in various high-temperature biotechnological processes. Biocatalysts of hyperthermophiles have proven to show extremely high thermo-activities and thermo-stabilities and are identified as suitable candidates for numerous industrial processes with harsh conditions, including the process of an efficient plant biomass pretreatment and conversion. Already-characterized archaea-originated glycoside hydrolases (GHs) have shown highly impressive features and numerous enzyme characterizations indicated that these biocatalysts show maximum activities at a higher temperature range compared to bacterial ones. However, compared to bacterial biomass-degrading enzymes, the number of characterized archaeal ones remains low. To discover new promising archaeal GH candidates, it is necessary to study in detail the microbiology and enzymology of extremely high-temperature habitats, ranging from terrestrial to marine hydrothermal systems. State-of-the art technologies such as sequencing of genomes and metagenomes and automated binning of genomes out of metagenomes, combined with classical microbiological culture-dependent approaches, have been successfully performed to detect novel promising biomass-degrading hyperthermozymes. In this review, we will focus on the detection, characterization and similarities of archaeal GHs and their unique characteristics. The potential of hyperthermozymes and their impact on high-temperature industrial applications have not yet been exhausted.

Indexed as

ArchaeaBioeconomyGlycoside hydrolasesHydrothermal systemsHyperthermozymes

Identifiers

PMID32905355
PMCPMC7469102
OpenAlexW3082234861

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.