Evidence map›Paper›PMID 28546828›Full record

ArticleBiotechnology for biofuels2017

Improving the thermostability of a fungal GH11 xylanase via site-directed mutagenesis guided by sequence and structural analysis.

Nanyu Han, Huabiao Miao, Junmei Ding, Junjun Li, Yuelin Mu, Junpei Zhou, Zunxi Huang

Open access · goldAbstract read
In one paragraph

Article in Biotechnology for biofuels, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

20 citing papers in PubMed, 59 citations in OpenAlex.

  1. Systematic optimization ofEngineering microbiology · 2026
    Review
  2. Review
  3. Article
  4. PEGASUS: Prediction of MD-derived protein flexibility from sequence.Protein science : a publication of the Protein Society · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Bioengineered Enzymes and Precision Fermentation in the Food Industry.International journal of molecular sciences · 2023
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Improving the Thermostability ofFrontiers in microbiology · 2020
    Article
  17. Transcriptomic Analysis ofFrontiers in microbiology · 2020
    Article
  18. Article
  19. Review
  20. 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

7 authors at 1 institution in 1 country.

Nanyu Han *School of Life Sciences, Yunnan Normal University, Kunming, 650500 China.
Huabiao Miao *School of Life Sciences, Yunnan Normal University, Kunming, 650500 China.
Junmei DingSchool of Life Sciences, Yunnan Normal University, Kunming, 650500 China.
Junjun LiSchool of Life Sciences, Yunnan Normal University, Kunming, 650500 China.
Yuelin MuSchool of Life Sciences, Yunnan Normal University, Kunming, 650500 China.
Junpei ZhouSchool of Life Sciences, Yunnan Normal University, Kunming, 650500 China.
Zunxi HuangSchool of Life Sciences, Yunnan Normal University, Kunming, 650500 China.
Yunnan Normal University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundXylanases have been widely employed in many industrial processes, and thermophilic xylanases are in great demand for meeting the high-temperature requirements of biotechnological treatments. In this work, we aim to improve the thermostability of XynCDBFV, a glycoside hydrolase (GH) family 11 xylanase from the ruminal fungus

resultsC-terminal residues 207-NGGA-210 in XynCDBFV were discovered to exhibit pronounced flexibility based on comparison of normalized B-factors. Multiple sequence alignment revealed that beneficial residues 207-SSGS-210 are highly conserved in GH11 xylanases. Thus, a recombinant xylanase, Xyn-MUT, was constructed by substituting three residues (N207S, G208S, A210S) at the C-terminus of XynCDBFV. Xyn-MUT exhibited higher thermostability than XynCDBFV at ≥70 °C. Xyn-MUT showed promising improvement in residual activity with a thermal retention of 14% compared to that of XynCDBFV after 1 h incubation at 80 °C; Xyn-MUT maintained around 50% of the maximal activity after incubation at 95 °C for 1 h. Kinetic measurements showed that the recombinant Xyn-MUT had greater kinetic efficiency than XynCDBFV (

conclusionsThis is the first report for GH11 recombinant with improved thermostability based on C-terminus replacement. The resulting Xyn-MUT will be an attractive candidate for industrial applications.

Indexed as

B-factorC-terminus replacementMD simulationSite-directed mutagenesisThermostabilityXylanase

Identifiers

PMID28546828
PMCPMC5442702
OpenAlexW2617474577

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.