ArticleJournal of industrial microbiology & biotechnology2012
Amino acid substitutions in the N-terminus, cord and α-helix domains improved the thermostability of a family 11 xylanase XynR8.
Article in Journal of industrial microbiology & biotechnology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 25 citations in OpenAlex.
- Review of Xylanases: Sources, Engineering and Biotechnological Use.Microorganisms · 2026Review
- Analyzing Current Trends and Possible Strategies to Improve Sucrose Isomerases' Thermostability.International journal of molecular sciences · 2023Review
- Three Molecular Modification Strategies to Improve the Thermostability of Xylanase XynA fromFoods (Basel, Switzerland) · 2023Article
- N-Terminus-Mediated Solution Structure of Dimerization Domain of PRC1.Current issues in molecular biology · 2022Article
- Engineering mesophilic GH11 xylanase fromFrontiers in bioengineering and biotechnology · 2022Article
- Article
- A multi-functional genetic manipulation system and its use in high-level expression of a β-mannanase mutant with high specific activity in Pichia pastoris.Microbial biotechnology · 2021Article
- Multiple Tolerance and Dye Decolorization Ability of a Novel Laccase Identified fromJournal of microbiology and biotechnology · 2020Article
- Mutational Mtc6p attenuates autophagy and improves secretory expression of heterologous proteins in Kluyveromyces marxianus.Microbial cell factories · 2018Article
- Simultaneous cell disruption and semi-quantitative activity assays for high-throughput screening of thermostable L-asparaginases.Scientific reports · 2018Article
- Article
- Structural Insight into and Mutational Analysis of Family 11 Xylanases: Implications for Mechanisms of Higher pH Catalytic Adaptation.PloS one · 2015Article
- Improvement in thermostability of metagenomic GH11 endoxylanase (Mxyl) by site-directed mutagenesis and its applicability in paper pulp bleaching process.Journal of industrial microbiology & biotechnology · 2013Article
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5 authors at 1 institution in 1 country.
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Abstract
The thermostability of xylanase XynR8 from uncultured Neocallimastigales rumen fungal was improved by combining random point mutagenesis with site-directed mutagenesis guided by rational design, and a thermostable variant, XynR8_VNE, was identified. This variant contained three amino acid substitutions, I38V, D137N and G151E, and showed an increased melting temperature of 8.8 °C in comparison with the wild type. At 65 °C the wild-type enzyme lost all of its activity after treatment for 30 min, but XynR8_VNE retained about 65 % activity. To elucidate the mechanism of thermal stabilization, three-dimensional structures were predicted for XynR8 and its variant. We found that the tight packing density and new salt bridge caused by the substitutions may be responsible for the improved thermostability. These three substitutions are located in the N-terminus, cord and α-helix domains, respectively. Hence, the stability of these three domains may be crucial for the thermostability of family 11 xylanases.
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