Evidence map›Paper›PMID 34613758›Full record

ArticleApplied and environmental microbiology2021

A Novel Multifunctional Arabinofuranosidase/Endoxylanase/β-Xylosidase GH43 Enzyme from Paenibacillus curdlanolyticus B-6 and Its Synergistic Action To Produce Arabinose and Xylose from Cereal Arabinoxylan.

Puangpen Limsakul, Paripok Phitsuwan, Rattiya Waeonukul, Patthra Pason, Chakrit Tachaapaikoon, Kanokwan Poomputsa, Akihiko Kosugi, Khanok Ratanakhanokchai

Open access · greenAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

11 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Review
  3. Non-Catalytic Domains of Glycoside Hydrolase Family 5 fromJournal of microbiology and biotechnology · 2025
    Article
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  8. Plastid Transformation: New Challenges in the Circular Economy Era.International journal of molecular sciences · 2022
    Review
  9. 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

8 authors at 2 institutions in 2 countries.

Puangpen LimsakulSchool of Bioresources and Technology, King Mongkut's University of Technology Thonburi, Bangkok, Thailand.
Paripok PhitsuwanSchool of Bioresources and Technology, King Mongkut's University of Technology Thonburi, Bangkok, Thailand.
Rattiya WaeonukulSchool of Bioresources and Technology, King Mongkut's University of Technology Thonburi, Bangkok, Thailand.
Patthra PasonSchool of Bioresources and Technology, King Mongkut's University of Technology Thonburi, Bangkok, Thailand.
Chakrit TachaapaikoonSchool of Bioresources and Technology, King Mongkut's University of Technology Thonburi, Bangkok, Thailand.
Kanokwan PoomputsaSchool of Bioresources and Technology, King Mongkut's University of Technology Thonburi, Bangkok, Thailand.
Akihiko KosugiBiological Resources and Post-harvest Division, Japan International Research Center for Agricultural Sciencesgrid.452611.5, Ibaraki, Japan.
Khanok RatanakhanokchaiSchool of Bioresources and Technology, King Mongkut's University of Technology Thonburi, Bangkok, Thailand.ORCID 0000-0002-8473-1294
King Mongkut's University of Technology Thonburi · THJapan International Research Center for Agricultural Sciences · JP

Funding

Thailand Research Fund PHD/0106/2553
6 · The paper itself

Abstract

PcAxy43B is a modular protein comprising a catalytic domain of glycoside hydrolase family 43 (GH43), a family 6 carbohydrate-binding module (CBM6), and a family 36 carbohydrate-binding module (CBM36) and found to be a novel multifunctional xylanolytic enzyme from Paenibacillus curdlanolyticus B-6. This enzyme exhibited α-l-arabinofuranosidase, endoxylanase, and β-d-xylosidase activities. The α-l-arabinofuranosidase activity of PcAxy43B revealed a new property of GH43, via the release of both long-chain cereal arabinoxylan and short-chain arabinoxylooligosaccharide (AXOS), as well as release from both the C(O)

Indexed as

Endo-1,4-beta XylanasesXylansArabinoseBacterial ProteinsEdible GrainGlycoside HydrolasesMultifunctional EnzymesPaenibacillusXyloseXylosidasesArabinosearabinoxylanBacterial ProteinsEndo-1,4-beta Xylanasesexo-1,4-beta-D-xylosidaseGlycoside HydrolasesMultifunctional EnzymesXylansXyloseXylosidasescarbohydrate-binding modulecereal arabinoxylancereal biomassglycoside hydrolase family 43multifunctional xylanolytic enzymePaenibacillus curdlanolyticusα-l-arabinofuranosidase/endoxylanase/β-xylosidase activities

Identifiers

PMID34613758
PMCPMC8612256
OpenAlexW3204376229

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.