Evidence map›Paper›PMID 38884653›Full record

ArticleArchives of microbiology2024

Identification of a novel glycoside hydrolase family 8 xylanase from Deinococcus geothermalis and its application at low temperatures.

Tingting Wang, Min Lin, Yongliang Yan, Shijie Jiang, Qilin Dai, Zhengfu Zhou, Jin Wang

Abstract read
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Article in Archives of microbiology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
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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

7 authors.

Tingting WangCollege of Life Science and Engineering, Southwest University of Science and Technology, Mianyang, 621000, China.
Min LinCollege of Life Science and Engineering, Southwest University of Science and Technology, Mianyang, 621000, China.
Yongliang YanNational Key Laboratory of Agricultural Microbiology, Biotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing, 100081, China.
Shijie JiangCollege of Life Science and Engineering, Southwest University of Science and Technology, Mianyang, 621000, China.
Qilin DaiCollege of Life Science and Engineering, Southwest University of Science and Technology, Mianyang, 621000, China.
Zhengfu ZhouNational Key Laboratory of Agricultural Microbiology, Biotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing, 100081, China. zhouzhengfu@caas.cn.
Jin WangCollege of Life Science and Engineering, Southwest University of Science and Technology, Mianyang, 621000, China.

Funding

Agricultural Science and Technology Innovation Program of the Chinese Academy of Agricultural Sciences CAAS-ZDRW202305National Key R&D Program of China 2023YFF1000300National Natural Science Foundation of China 31930004National Natural Science Foundation of China 32270067Third Xinjiang Scientific Expedition 2022xjkk020602
6 · The paper itself

Abstract

Xylanase is the most important hydrolase in the xylan hydrolase system, the main function of which is β-1,4-endo-xylanase, which randomly cleaves xylans to xylo-oligosaccharides and xylose. Xylanase has wide ranging of applications, but there remains little research on the cold-adapted enzymes required in some low-temperature industries. Glycoside hydrolase family 8 (GH8) xylanases have been reported to have cold-adapted enzyme activity. In this study, the xylanase gene dgeoxyn was excavated from Deinococcus geothermalis through sequence alignment. The recombinant xylanase DgeoXyn encodes 403 amino acids with a theoretical molecular weight of 45.39 kDa. Structural analysis showed that DgeoXyn has a (α/α)6-barrel fold structure typical of GH8 xylanase. At the same time, it has strict substrate specificity, is only active against xylan, and its hydrolysis products include xylobiose, xylotrinose, xytetranose, xylenanose, and a small amount of xylose. DgeoXyn is most active at 70 ℃ and pH 6.0. It is very stable at 10, 20, and 30 ℃, retaining more than 80% of its maximum enzyme activity. The enzyme activity of DgeoXyn increased by 10% after the addition of Mn

Indexed as

DeinococcusEndo-1,4-beta XylanasesEnzyme StabilityXylansAmino Acid SequenceBacterial ProteinsCloning, MolecularCold TemperatureDisaccharidesGlycoside HydrolasesHydrogen-Ion ConcentrationHydrolysisKineticsMolecular WeightRecombinant ProteinsSequence AlignmentBacterial ProteinsDisaccharidesEndo-1,4-beta XylanasesGlycoside HydrolasesRecombinant ProteinsXylansxylobioseCold-adapted enzymeDeinococcus geothermalisDgeoXynGH8Xylanase

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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.