Evidence map›Paper›PMID 24212471›Full record

ArticleJournal of industrial microbiology & biotechnology2014

Improvement of alkali stability and thermostability of Paenibacillus campinasensis Family-11 xylanase by directed evolution and site-directed mutagenesis.

Hongchen Zheng, Yihan Liu, Mingzhe Sun, Yang Han, Jianling Wang, Junshe Sun, Fuping Lu

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Article in Journal of industrial microbiology & biotechnology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

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12citing papers in PubMed
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3 · Its place in the literature

Who cites it

12 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Directed evolution of a β-mannanase fromBiotechnology for biofuels · 2017
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
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5 · Who and what money

Authors and funding

7 authors.

Hongchen ZhengKey Laboratory of Industrial Fermentation Microbiology, Education Ministry of China, Tianjin, 300457, China.
Yihan Liu
Mingzhe Sun
Yang Han
Jianling Wang
Junshe Sun
Fuping Lu

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The extreme process condition of high temperature and high alkali limits the applications of most of natural xylanases in pulp and paper industry. Recently, various methods of protein engineering have been used to improve the thermal and alkalic tolerance of xylanases. In this work, directed evolution and site-directed mutagenesis were performed to obtain a mutant xylanase improved both on alkali stability and thermostability from the native Paenibacillus campinasensis Family-11 xylanase (XynG1-1). Mutant XynG1-1B43 (V90R/P172H) with two units increased in the optimum pH (pH 7.0-pH 9.0) and significant improvement on alkali stability was selected from the second round of epPCR library. And the further thermoduric mutant XynG1-1B43cc16 (V90R/P172H/T84C-T182C/D16Y) with 10 °C increased in the optimum temperature (60-70 °C) was then obtained by introducing a disulfide bridge (T84C-T182C) and a single amino acid substitution (D16Y) to XynG1-1B43 using site-directed mutagenesis. XynG1-1B43cc16 also showed higher thermostability and catalytic efficiency (k cat /K m ) than that of wild-type (XynG1-1) and XynG1-1B43. The attractive improved properties make XynG1-1B43cc16 more suitable for bioleaching of cotton stalk pulp under the extreme process condition of high temperature (70 °C) and high alkali (pH 9.0).

Indexed as

AlkaliesAmino Acid SequenceAmino Acid SubstitutionDirected Molecular EvolutionDisulfidesEndo-1,4-beta XylanasesEnzyme StabilityGene LibraryHot TemperatureHydrogen-Ion ConcentrationMolecular Sequence DataMutagenesis, Site-DirectedPaenibacillusSequence AlignmentAlkaliesDisulfidesEndo-1,4-beta Xylanases

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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.