Evidence map›Paper›PMID 29783967›Full record

ArticleBMC biotechnology2018

Characterization of a novel thermostable and xylose-tolerant GH 39 β-xylosidase from Dictyoglomus thermophilum.

Qi Li, Tao Wu, Zhipeng Qi, Linguo Zhao, Jianjun Pei, Feng Tang

Open access · goldAbstract read
In one paragraph

Article in BMC biotechnology, 2018. 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
2.0field-weighted citation impact, top 14% 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, 45 citations in OpenAlex.

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  9. RSC advances · 2022
    Article
  10. Biochemical Basis of Xylooligosaccharide Utilisation by Gut Bacteria.International journal of molecular sciences · 2022
    Article
  11. 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

6 authors at 3 institutions in 1 country.

Qi LiCo-Innovation Center for Sustainable Forestry in Southern China, Nanjing Forestry University, 159 Long Pan Road, Nanjing, 210037, China.
Tao WuCollege of Chemical Engineering, Nanjing Forestry University, 159 Long Pan Road, Nanjing, 210037, China.
Zhipeng QiCollege of Chemical Engineering, Nanjing Forestry University, 159 Long Pan Road, Nanjing, 210037, China.
Linguo ZhaoCo-Innovation Center for Sustainable Forestry in Southern China, Nanjing Forestry University, 159 Long Pan Road, Nanjing, 210037, China. njfu2304@163.com.
Jianjun PeiCollege of Chemical Engineering, Nanjing Forestry University, 159 Long Pan Road, Nanjing, 210037, China.
Feng TangInternational Centre for Bamboo and Rattan, 8 Fu Tong East Street, Beijing, 100714, China.
Nanjing Forestry University · CNInstitute of Chemical Industry of Forest Products · CNInternational Bamboo and Rattan Organization · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundβ-D-xylosidase is a vital exoglycosidase with the ability to hydrolyze xylooligosaccharides to xylose and to biotransform some saponins by cleaving outer β-xylose. β-D-xylosidase is widely used as one of the xylanolytic enzymes in a diverse range of applications, such as fuel, food and the pharmaceutical industry; therefore, more and more studies have focused on the thermostable and xylose-tolerant β-D-xylosidases.

resultsA thermostable β-xylosidase gene (xln-DT) of 1509 bp was cloned from Dictyoglomus thermophilum and expressed in E.coli BL21. According to the amino acid and phylogeny analyses, the β-xylosidase Xln-DT is a novel β-xylosidase of the GH family 39. The recombinant β-xylosidase was purified, showing unique bands on SDS-PAGE, and had a protein molecular weight of 58.7 kDa. The β-xylosidase Xln-DT showed an optimal activity at pH 6.0 and 75 °C, with p-nitrophenyl-β-D-xylopyranoside (pNPX) as a substrate. Xln-DT displayed stability over a pH range of 4.0-7.5 for 24 h and displayed thermotolerance below 85 °C. The values of the kinetic parameters K

conclusionThis study provides a novel GH 39 β-xylosidase displaying extraordinary properties of highly catalytic activity at temperatures above 75 °C, remarkable hydrolyzing activity of xylooligosaccharides and rare saponins producing ability in the pharmaceutical and commercial industries.

Indexed as

Bacterial ProteinsEnzyme StabilityGlucuronatesHot TemperatureHydrogen-Ion ConcentrationKineticsOligosaccharidesSubstrate SpecificityXyloseXylosidasesBacterial Proteinsexo-1,4-beta-D-xylosidaseGlucuronatesOligosaccharidesxylooligosaccharideXyloseXylosidasesBiotransformationDictyoglomus thermophilumXylooligosaccharidesXylose tolerantβ-xylosidase

Identifiers

PMID29783967
PMCPMC5963010
OpenAlexW2807465248

What OpenQuestion holds

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LicenceCC BY
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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.