Evidence map›Paper›PMID 34142143›Full record

ArticleGlycobiology2021

Novel xylan-degrading enzymes from polysaccharide utilizing loci of Prevotella copri DSM18205.

Javier A Linares-Pastén, Johan Sebastian Hero, José Horacio Pisa, Cristina Teixeira, Margareta Nyman, Patrick Adlercreutz, M Alejandra Martinez, Eva Nordberg Karlsson

Open access · hybridAbstract read
In one paragraph

Article in Glycobiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.2field-weighted citation impact, top 24% 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

15 citing papers in PubMed, 19 citations in OpenAlex.

  1. Bridging the gap:Gut microbes · 2026
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  7. Daily fluctuation of genusFrontiers in microbiology · 2025
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  11. Article
  12. Frontiers in nutrition · 2022
    Article
  13. Understanding the Role ofAnimals : an open access journal from MDPI · 2021
    Article
  14. Review
  15. Review
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

8 authors at 3 institutions in 2 countries.

Javier A Linares-PasténBiotechnology, Department of Chemistry, Lund University, P.O. Box 124, 221 00 Lund, Sweden.ORCID 0000-0001-6999-6334
Johan Sebastian HeroPlanta Piloto de Procesos Industriales Microbiológicos PROIMI-CONICET, Av. Belgrano y Pasaje Caseros, T4001 MVB San Miguel de Tucumán, Argentina.ORCID 0000-0002-3905-3666
José Horacio PisaPlanta Piloto de Procesos Industriales Microbiológicos PROIMI-CONICET, Av. Belgrano y Pasaje Caseros, T4001 MVB San Miguel de Tucumán, Argentina.
Cristina TeixeiraBiotechnology, Department of Chemistry, Lund University, P.O. Box 124, 221 00 Lund, Sweden.ORCID 0000-0002-1382-1671
Margareta NymanDepartment of Food Technology, Engineering and Nutrition, Lund University, P.O. Box 124, SE-221 00 Lund, Sweden.
Patrick AdlercreutzBiotechnology, Department of Chemistry, Lund University, P.O. Box 124, 221 00 Lund, Sweden.
M Alejandra MartinezPlanta Piloto de Procesos Industriales Microbiológicos PROIMI-CONICET, Av. Belgrano y Pasaje Caseros, T4001 MVB San Miguel de Tucumán, Argentina.ORCID 0000-0002-9250-3486
Eva Nordberg KarlssonBiotechnology, Department of Chemistry, Lund University, P.O. Box 124, 221 00 Lund, Sweden.ORCID 0000-0002-8597-7050
Lund University · SEConsejo Nacional de Investigaciones Científicas y Técnicas · ARNational University of Tucumán · AR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Prevotella copri is a bacterium that can be found in the human gastrointestinal tract (GIT). The role of P. copri in the GIT is unclear, and elevated numbers of the microbe have been reported both in dietary fiber-induced improvement in glucose metabolism but also in conjunction with certain inflammatory conditions. These findings raised our interest in investigating the possibility of P. copri to grow on xylan, and identify the enzyme systems playing a role in digestion of xylan-based dietary fibers. Two xylan degrading polysaccharide utilizing loci (PUL10 and 15) were found in the genome, with three and eight glycoside hydrolase (GH) -encoding genes, respectively. Three of them were successfully produced in Escherichia coli: One extracellular enzyme from GH43 (subfamily 12, in PUL10, 60 kDa) and two enzymes from PUL15, one extracellular GH10 (41 kDa), and one intracellular GH43 (subfamily 137 kDa). Based on our results, we propose that in PUL15, GH10 (1) is an extracellular endo-1,4-β-xylanase, that hydrolazes mainly glucuronosylated xylan polymers to xylooligosaccharides (XOS); while, GH43_1 in the same PUL, is an intracellular β-xylosidase, catalyzing complete hydrolysis of the XOS to xylose. In PUL10, the characterized GH43_12 is an arabinofuranosidase, with a role in degradation of arabinoxylan, catalyzing removal of arabinose-residues on xylan.

Indexed as

Glycoside HydrolasesKineticsModels, MolecularPolysaccharidesPrevotellaXylansGlycoside HydrolasesPolysaccharidesXylansarabinofuranosidasepolysaccharide utilizing lociPrevotella coprixylanase xylosidase

Identifiers

PMID34142143
PMCPMC8631079
OpenAlexW3169916393

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.