Evidence map›Paper›PMID 31728656›Full record

ReviewWorld journal of microbiology & biotechnology2019

A mini review of xylanolytic enzymes with regards to their synergistic interactions during hetero-xylan degradation.

Samkelo Malgas, Mpho S Mafa, Lithalethu Mkabayi, Brett I Pletschke

Abstract readReview
PubMed Publisher
In one paragraph

Review in World journal of microbiology & biotechnology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
6.4field-weighted citation impact, top 3% 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

39 citing papers in PubMed, 124 citations in OpenAlex.

  1. Review
  2. Endo-β-1,4-Xylanase GH10 fromInternational journal of molecular sciences · 2026
    Article
  3. Article
  4. Enzymatic production of prebiotic xylooligosaccharides.World journal of microbiology & biotechnology · 2026
    Review
  5. A single-domain expansin-like protein fromProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Article
  7. Annotated draft genome data ofData in brief · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Expression inInternational journal of molecular sciences · 2024
    Article
  12. Article
  13. Article
  14. Contribution of Microbiota to Bioactivity Exerted by Bee Bread.Pharmaceuticals (Basel, Switzerland) · 2024
    Article
  15. Review
  16. Article
  17. Plastid Transformation: New Challenges in the Circular Economy Era.International journal of molecular sciences · 2022
    Review
  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 2 institutions in 1 country.

Samkelo MalgasEnzyme Science Programme (ESP), Department of Biochemistry and Microbiology, Rhodes University, Grahamstown, Eastern Cape, 6140, South Africa.ORCID http://orcid.org/0000-0003-0729-5393
Mpho S MafaEnzyme Science Programme (ESP), Department of Biochemistry and Microbiology, Rhodes University, Grahamstown, Eastern Cape, 6140, South Africa.ORCID http://orcid.org/0000-0003-2385-4423
Lithalethu MkabayiEnzyme Science Programme (ESP), Department of Biochemistry and Microbiology, Rhodes University, Grahamstown, Eastern Cape, 6140, South Africa.ORCID http://orcid.org/0000-0001-7620-5596
Brett I PletschkeEnzyme Science Programme (ESP), Department of Biochemistry and Microbiology, Rhodes University, Grahamstown, Eastern Cape, 6140, South Africa. b.pletschke@ru.ac.za.ORCID http://orcid.org/0000-0001-8117-1730
Rhodes University · ZAUniversity of the Witwatersrand · ZA

Funding

Department of Science and Technology, Republic of South Africa DST National Biocatalysis Initiative ProjectNational Research Foundation PhD bursary (Innovation)Rhodes University Sandisa Imbewu
6 · The paper itself

Abstract

This review examines the recent models describing the mode of action of various xylanolytic enzymes and how these enzymes can be applied (sequentially or simultaneously) with their distinctive roles in mind to achieve efficient xylan degradation. With respect to homeosynergy, synergism appears to be as a result of β-xylanase and/or oligosaccharide reducing-end β-xylanase liberating xylo-oligomers (XOS) that are preferred substrates of the processive β-xylosidase. With regards to hetero-synergism, two cross relationships appear to exist and seem to be the reason for synergism between the enzymes during xylan degradation. These cross relations are the debranching enzymes such as α-glucuronidase or side-chain cleaving enzymes such as carbohydrate esterases (CE) removing decorations that would have hindered back-bone-cleaving enzymes, while backbone-cleaving-enzymes liberate XOS that are preferred substrates of the debranching and side-chain-cleaving enzymes. This interaction is demonstrated by high yields in co-production of xylan substituents such as arabinose, glucuronic acid and ferulic acid, and XOS. Finally, lytic polysaccharide monooxygenases (LPMO) have also been implicated in boosting whole lignocellulosic biomass or insoluble xylan degradation by glycoside hydrolases (GH) by possibly disrupting entangled xylan residues. Since it has been observed that the same enzyme (same Enzyme Commission, EC, classification) from different GH or CE and/or AA families can display different synergistic interactions with other enzymes due to different substrate specificities and properties, in this review, we propose an approach of enzyme selection (and mode of application thereof) during xylan degradation, as this can improve the economic viability of the degradation of xylan for producing precursors of value added products.

Indexed as

ArabinoseBiodegradation, EnvironmentalCoumaric AcidsEndo-1,4-beta XylanasesEsterasesGlucuronic AcidGlycoside HydrolasesOligosaccharidesPolysaccharidesSubstrate SpecificityXylansXylosidasesalpha-glucuronidaseArabinoseCoumaric AcidsEndo-1,4-beta XylanasesEsterasesexo-1,4-beta-D-xylosidaseferulic acidGlucuronic AcidGlycoside HydrolasesOligosaccharidesPolysaccharidesXylansXylosidasesCarbohydrate esterasesDegradationGlycoside hydrolasesLytic polysaccharide monooxygenaseSynergyXylan

Identifiers

PMID31728656
OpenAlexW2987131365

What OpenQuestion holds

Textmetadata
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.