ArticleJournal of industrial microbiology & biotechnology2007
Introduction of a disulfide bridge enhances the thermostability of a Streptomyces olivaceoviridis xylanase mutant.
Article in Journal of industrial microbiology & biotechnology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Review of Xylanases: Sources, Engineering and Biotechnological Use.Microorganisms · 2026Review
- Three Molecular Modification Strategies to Improve the Thermostability of Xylanase XynA fromFoods (Basel, Switzerland) · 2023Article
- Mutagenesis of N-terminal residues confer thermostability on a Penicillium janthinellum MA21601 xylanase.BMC biotechnology · 2019Article
- Design, expression and functional characterization of a thermostable xylanase from Trichoderma reesei.PloS one · 2019Article
- Engineering and introduction of de novo disulphide bridges in organophosphorus hydrolase enzyme for thermostability improvement.Journal of biosciences · 2016Article
- Structure of a His170Tyr mutant of thermostable pNPPase from Geobacillus stearothermophilus.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Improvement of alkali stability and thermostability of Paenibacillus campinasensis Family-11 xylanase by directed evolution and site-directed mutagenesis.Journal of industrial microbiology & biotechnology · 2014Article
- Amino acid substitutions in the N-terminus, cord and α-helix domains improved the thermostability of a family 11 xylanase XynR8.Journal of industrial microbiology & biotechnology · 2012Article
- Characteristics of bifunctional acidic endoglucanase (Cel5B) from Gloeophyllum trabeum.Journal of industrial microbiology & biotechnology · 2012Article
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6 authors.
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Abstract
Substitution of the N-terminus of Streptomyces olivaceoviridis xylanase XYNB to generate mutant TB has been previously shown to increase the thermostability of the enzyme. To further improve the stability of this mutant, we introduced a disulfide bridge (C109-C153) into the TB mutant, generating TS. To assess the effect of the disulfide bridge in the wild-type enzyme, the S109C-N153C mutation was also introduced into XYNB, resulting in XS. The mutants were expressed in Pichia pastoris, the recombinant enzymes were purified, and the effect of temperature and pH on enzymatic activity was characterized. Introduction of the disulfide bridge (C109-C153) into XYNB (XS variant) and TB (TS variant) increased the thermostability up to 2.8-fold and 12.4-fold, respectively, relative to XYNB, after incubation at 70 degrees C, pH 6.0, for 20 min. In addition, a synergistic effect of the disulfide bridge and the N-terminus replacement was observed, which extended the half-life of XYNB from 3 to 150 min. Moreover, XS and TS displayed better resistance to acidic conditions compared with the respective enzymes that did not contain a disulfide bridge.
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