Evidence map›Paper›PMID 34718907›Full record

ArticleBiotechnology letters2021

Biochemical characterization of xylanase GH11 isolated from Aspergillus niger BCC14405 (XylB) and its application in xylooligosaccharide production.

Katesuda Aiewviriyasakul, Benjarat Bunterngsook, Hataikarn Lekakarn, Wipawee Sritusnee, Pattanop Kanokratana, Verawat Champreda

Abstract read
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Article in Biotechnology letters, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

5 citing papers in PubMed, 18 citations in OpenAlex.

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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

6 authors at 2 institutions in 1 country.

Katesuda AiewviriyasakulEnzyme Technology Research Team, Biorefinery Technology and Bioproduct Research Group, National Center for Genetic Engineering and Biotechnology, 113 Thailand Science Park, Phahonyothin Road, Khlong Luang, Pathumthani, 12120, Thailand.
Benjarat BunterngsookEnzyme Technology Research Team, Biorefinery Technology and Bioproduct Research Group, National Center for Genetic Engineering and Biotechnology, 113 Thailand Science Park, Phahonyothin Road, Khlong Luang, Pathumthani, 12120, Thailand. benjarat.bun@biotec.or.th.ORCID http://orcid.org/0000-0002-6741-684X
Hataikarn LekakarnDepartment of Biotechnology, Faculty of Science and Technology, Thammasat University, Rangsit Campus, Phahonyothin Road, Khlong Luang, Pathumthani, 12120, Thailand.
Wipawee SritusneeEnzyme Technology Research Team, Biorefinery Technology and Bioproduct Research Group, National Center for Genetic Engineering and Biotechnology, 113 Thailand Science Park, Phahonyothin Road, Khlong Luang, Pathumthani, 12120, Thailand.
Pattanop KanokratanaEnzyme Technology Research Team, Biorefinery Technology and Bioproduct Research Group, National Center for Genetic Engineering and Biotechnology, 113 Thailand Science Park, Phahonyothin Road, Khlong Luang, Pathumthani, 12120, Thailand.
Verawat ChampredaEnzyme Technology Research Team, Biorefinery Technology and Bioproduct Research Group, National Center for Genetic Engineering and Biotechnology, 113 Thailand Science Park, Phahonyothin Road, Khlong Luang, Pathumthani, 12120, Thailand.
National Center for Genetic Engineering and Biotechnology · THThammasat University · TH

Funding

National Science and Technology Development Agency P18-52705
6 · The paper itself

Abstract

objectiveTo develop an endo-β-1,4-xylanase with high specificity for production of prebiotic xylooligosaccharides that optimally works at moderate temperature desirable to reduce the energy cost in the production process.

resultsThe xylB gene, encoding for a glycosyl hydrolase family 11 xylanase from a thermoresistant fungus, Aspergillus niger BCC14405 was expressed in a methylotrophic yeast P. pastoris KM71 in a secreted form. The recombinant XylB showed a high specific activity of 3852 and 169 U mg

conclusionThe enzyme is potent for XOS production and for saccharification of lignocellulosic biomass.

Indexed as

Aspergillus nigerEndo-1,4-beta XylanasesEnzyme StabilityGlucuronatesHydrogen-Ion ConcentrationHydrolysisOligosaccharidesSubstrate SpecificityTemperatureXylansarabinoxylanEndo-1,4-beta XylanasesGlucuronatesOligosaccharidesXylansxylooligosaccharideAspergillus nigerGlycosyl hydrolaseLignocelluloseXylanaseXylooligosaccharides

Identifiers

PMID34718907
OpenAlexW3209365923

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.