Evidence map›Paper›PMID 41501755›Full record

ArticleBMC biotechnology2026

Molecular cloning and characterization of a GH10 thermophilic xylanase from hot spring and its potential application in promoting probiotic growth.

Jian-Ling Li, Wei Hu, Lan-Hua Pu, Jing Sun, Maite Ortúzar, Zhi-Hua Lv, Zheng-Feng Yang, Dan Zhu, Kai-Qing Xie, Li-Quan Yang and 1 more

Abstract read
In one paragraph

Article in BMC biotechnology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. Review
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

11 authors.

Jian-Ling Li *College of Agriculture and Biological Science, Dali University, Dali, 671003, P. R. China.
Wei Hu *College of Agriculture and Biological Science, Dali University, Dali, 671003, P. R. China.
Lan-Hua PuCollege of Agriculture and Biological Science, Dali University, Dali, 671003, P. R. China.
Jing SunCollege of Agriculture and Biological Science, Dali University, Dali, 671003, P. R. China.
Maite Ortúzar *State Key Laboratory of Biocontrol, Guangdong Provincial Key Laboratory of Plant Resources and Southern Marine Science and Engineering Guangdong Laboratory (Zhuhai), School of Life Sciences, Sun Yat-Sen University, Guangzhou, China.
Zhi-Hua LvCollege of Agriculture and Biological Science, Dali University, Dali, 671003, P. R. China.
Zheng-Feng YangCollege of Agriculture and Biological Science, Dali University, Dali, 671003, P. R. China.
Dan ZhuCollege of Agriculture and Biological Science, Dali University, Dali, 671003, P. R. China.
Kai-Qing XieCollege of Agriculture and Biological Science, Dali University, Dali, 671003, P. R. China.
Li-Quan YangCollege of Agriculture and Biological Science, Dali University, Dali, 671003, P. R. China. ylqbioinfo@163.com.
Yi-Rui YinCollege of Agriculture and Biological Science, Dali University, Dali, 671003, P. R. China. yinyirui@dali.edu.cn.

Funding

the Xingdian Talent Support Program of Yunnan Province 230212528080Yunnan Applied Basic Research Projects 202101AU070138 and 202501AT070411
6 · The paper itself

Abstract

backgroundXylan is widely found in plant cell walls, and xylanase, an essential enzyme in xylan breakdown, has promising applications in energy, food, feed, and healthcare sectors.

resultsThis study presents the discovery of a novel GH10 family xylanase gene, termed Lc-Xyn81, isolated from the hot spring of Eryuan, Dali, Yunnan Province, employing enrichment culture and metagenomic approaches. The amino acid sequence of Lc-Xyn81 shares 72.29% identity with that of Blastocatellia bacterium. The gene was amplified via specific PCR, cloned, and heterologously expressed in Escherichia coli. The recombinant Lc-Xyn81 was purified using Ni-affinity chromatography, followed by enzymatic characterization. Lc-Xyn81 demonstrated optimal activity at 75 °C and pH 6.6. It maintained over 80% relative activity between 65 and 75 °C, and its activity increased to over 120% after incubation at 70 °C for 40–100 min with a half-life of 180 min at 70 °C. Additionally, incubation at pH 5.0–7.0 for 12 h boosted its activity to over 140%. Lc-Xyn81 was activated by divalent metal ions such as Co²⁺ (128.55%), Mn²⁺ (119.84%), and Cu²⁺ (112.27%). The enzyme exhibited activity against beechwood xylan (213.68 U/mg), corncob xylan (143.40 U/mg), and sugarcane bagasse xylan (80.39 U/mg). The primary degradation products were xylobiose and xylotetraose, which significantly promoted the growth of L. lactis. Kinetic analysis indicated that the Km value of Lc-Xyn81 for beechwood xylan is 4.62 mg/mL, and its Vmax value is 312.5 µmol/min/mg.

conclusionsIn summary, Lc-Xyn81, a thermophilic and thermostable xylanase, exhibits considerable potential for industrial applications in lignocellulose degradation and prebiotic production.

Indexed as

Bacterial ProteinsEndo-1,4-beta XylanasesHot SpringsAmino Acid SequenceCloning, MolecularDisaccharidesEnzyme StabilityEscherichia coliGlucuronatesHydrogen-Ion ConcentrationKineticsMolecular Sequence DataOligosaccharidesRecombinant ProteinsSubstrate SpecificityXylansBacterial ProteinsDisaccharidesEndo-1,4-beta XylanasesGlucuronatesOligosaccharidesRecombinant ProteinsXylansxylobiosexylooligosaccharideHot springsMetagenomicsThermophilicXylanaseXylooligosaccharides

Identifiers

PMID41501755
PMCPMC12870337

What OpenQuestion holds

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LicenceCC BY-NC-ND
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Registered trials

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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.