Evidence map›Paper›PMID 30196329›Full record

ReviewApplied microbiology and biotechnology2018

Endo-xylanases as tools for production of substituted xylooligosaccharides with prebiotic properties.

Eva Nordberg Karlsson, Eva Schmitz, Javier A Linares-Pastén, Patrick Adlercreutz

Open access · hybridAbstract readReview
In one paragraph

Review in Applied microbiology and biotechnology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
8.3field-weighted citation impact, top 2% 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

55 citing papers in PubMed, 205 citations in OpenAlex.

  1. Article
  2. Article
  3. Enzymatic production of prebiotic xylooligosaccharides.World journal of microbiology & biotechnology · 2026
    Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Discovery andACS omega · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. A novel glycoside hydrolase 43-like enzyme fromApplied and environmental microbiology · 2024
    Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  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

4 authors at 1 institution in 1 country.

Eva Nordberg KarlssonDivision of Biotechnology, Lund University, P.O.Box 124, 221 00, Lund, Sweden.
Eva SchmitzDivision of Biotechnology, Lund University, P.O.Box 124, 221 00, Lund, Sweden.
Javier A Linares-PasténDivision of Biotechnology, Lund University, P.O.Box 124, 221 00, Lund, Sweden.
Patrick AdlercreutzDivision of Biotechnology, Lund University, P.O.Box 124, 221 00, Lund, Sweden. Patrick.Adlercreutz@biotek.lu.se.ORCID http://orcid.org/0000-0001-9923-3397
Lund University · SE

Funding

VINNOVA 2017-02713
6 · The paper itself

Abstract

Xylan has a main chain consisting of β-1,4-linked xylose residues with diverse substituents. Endoxylanases cleave the xylan chain at cleavage sites determined by the substitution pattern and thus give different oligosaccharide product patterns. Most known endoxylanases belong to glycoside hydrolase (GH) families 10 and 11. These enzymes work well on unsubstituted xylan but accept substituents in certain subsites. The GH11 enzymes are more restricted by substituents, but on the other hand, they are normally more active than the GH10 enzymes on insoluble substrates, because of their smaller size. GH5 endoxylanases accept arabinose substituents in several subsites and require it in the - 1 subsite. This specificity makes the GH5 endoxylanases very useful for degradation of highly arabinose-substituted xylans and for the selective production of arabinoxylooligosaccharides, without formation of unsubstituted xylooligosaccharides. The GH30 endoxylanases have a related type of specificity in that they require a uronic acid substituent in the - 2 subsite, which makes them very useful for the production of uronic acid substituted oligosaccharides. The ability of dietary xylooligosaccharides to function as prebiotics in humans is governed by their substitution patterns. Endoxylanases are thus excellent tools to tailor prebiotic oligosaccharides to stimulate various types of intestinal bacteria and to cause fermentation in different parts of the gastrointestinal tract. Continuously increasing knowledge on the function of the gut microbiota and discoveries of novel endoxylanases increase the possibilities to achieve health-promoting effects.

Indexed as

ArabinoseEndo-1,4-beta XylanasesGastrointestinal MicrobiomeGastrointestinal TractGlucuronatesHumansOligosaccharidesPrebioticsSubstrate SpecificityUronic AcidsXylansArabinoseEndo-1,4-beta XylanasesGlucuronatesOligosaccharidesPrebioticsUronic AcidsXylansxylooligosaccharideArabinoseOligosaccharidePrebioticsUronic acidsXylanase

Identifiers

PMID30196329
PMCPMC6208967
OpenAlexW2890224301

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.