Evidence map›Paper›PMID 37749183›Full record

ArticleScientific reports2023

Characterization of a GH10 extremely thermophilic xylanase from the metagenome of hot spring for prebiotic production.

Yi-Rui Yin, Xin-Wei Li, Chao-Hua Long, Lei Li, Yu-Ying Hang, Meng-Di Rao, Xin Yan, Quan-Lin Liu, Peng Sang, Wen-Jun Li and 1 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 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

11 authors at 1 institution in 1 country.

Yi-Rui Yin *College of Agriculture and Biological Science, Dali University, Dali, 671003, People's Republic of China. yirui.yin@qq.com.
Xin-Wei Li *College of Agriculture and Biological Science, Dali University, Dali, 671003, People's Republic of China.
Chao-Hua LongCollege of Agriculture and Biological Science, Dali University, Dali, 671003, People's Republic of China.
Lei LiCollege of Agriculture and Biological Science, Dali University, Dali, 671003, People's Republic of China.
Yu-Ying HangCollege of Agriculture and Biological Science, Dali University, Dali, 671003, People's Republic of China.
Meng-Di RaoCollege of Agriculture and Biological Science, Dali University, Dali, 671003, People's Republic of China.
Xin YanCollege of Agriculture and Biological Science, Dali University, Dali, 671003, People's Republic of China.
Quan-Lin LiuCollege of Agriculture and Biological Science, Dali University, Dali, 671003, People's Republic of China.
Peng SangCollege of Agriculture and Biological Science, Dali University, Dali, 671003, People's Republic of China.
Wen-Jun LiCollege of Agriculture and Biological Science, Dali University, Dali, 671003, People's Republic of China. liwenjun3@mail.sysu.edu.cn.
Li-Quan YangCollege of Agriculture and Biological Science, Dali University, Dali, 671003, People's Republic of China. ylqbioinfo@163.com.
Dali University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A xylanase gene (named xyngmqa) was identified from the metagenomic data of the Gumingquan hot spring (92.5 °C, pH 9.2) in Tengchong City, Yunnan Province, southwest China. It showed the highest amino acid sequence identity (82.70%) to endo-1,4-beta-xylanase from Thermotoga caldifontis. A constitutive expression plasmid (denominated pSHY211) and double-layer plate (DLP) method were constructed for cloning, expression, and identification of the XynGMQA gene. The XynGMQA gene was synthesized and successfully expressed in Escherichia coli DH5α. XynGMQA exhibited optimal activity at 90 °C and pH 4.6, being thermostable by maintaining 100% of its activity after 2 h incubated at 80 °C. Interestingly, its enzyme activity was enhanced by high temperatures (70 and 80 °C) and low pH (3.0-6.0). About 150% enzyme activity was detected after incubation at 70 °C for 20 to 60 min or 80 °C for 10 to 40 min, and more than 140% enzyme activity after incubation at pH 3.0 to 6.0 for 12 h. Hydrolytic products of beechwood xylan with XynGMQA were xylooligosaccharides, including xylobiose (X2), xylotriose (X3), and xylotetraose (X4). These properties suggest that XynGMQA as an extremely thermophilic xylanase, may be exploited for biofuel and prebiotic production from lignocellulosic biomass.

Indexed as

Hot SpringsAmino Acid SequenceBiofuelsChinaEscherichia coliMetagenomeBiofuels

Identifiers

PMID37749183
PMCPMC10520001
OpenAlexW4387013030

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.