ArticlePloS one2014
Seven N-terminal residues of a thermophilic xylanase are sufficient to confer hyperthermostability on its mesophilic counterpart.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Three Molecular Modification Strategies to Improve the Thermostability of Xylanase XynA fromFoods (Basel, Switzerland) · 2023Article
- Characterization of a novel β-agarase from Antarctic macroalgae-associated bacteria metagenomic library and anti-inflammatory activity of the enzymatic hydrolysates.Frontiers in microbiology · 2022Article
- Breeding of a thermostable xylanase-producing strain ofFrontiers in bioengineering and biotechnology · 2022Article
- Article
- Mutagenesis of N-terminal residues confer thermostability on a Penicillium janthinellum MA21601 xylanase.BMC biotechnology · 2019Article
- Thermostability improvement of a Talaromyces leycettanus xylanase by rational protein engineering.Scientific reports · 2017Article
- Thermostable microbial xylanases for pulp and paper industries: trends, applications and further perspectives.World journal of microbiology & biotechnology · 2016Review
- Effect of Temperature on Xylanase II from Trichoderma reesei QM 9414: A Calorimetric, Catalytic, and Conformational Study.Enzyme research · 2014Article
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Authors and funding
4 authors.
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Abstract
Xylanases, and especially thermostable xylanases, are increasingly of interest for the deconstruction of lignocellulosic biomass. In this paper, the termini of a pair of xylanases, mesophilic SoxB and thermophilic TfxA, were studied. Two regions in the N-terminus of TfxA were discovered to be potentially important for the thermostability. By focusing on Region 4, it was demonstrated that only two mutations, N32G and S33P cooperated to improve the thermostability of mesophilic SoxB. By introducing two potential regions into SoxB in combination, the most thermostable mutant, M2-N32G-S33P, was obtained. The M2-N32G-S33P had a melting temperature (Tm) that was 25.6°C higher than the Tm of SoxB. Moreover, M2-N32G-S33P was even three-fold more stable than TfxA and had a Tm value that was 9°C higher than the Tm of TfxA. Thus, for the first time, the mesophilic SoxB "pupil" outperformed its thermophilic TfxA "master" and acquired hyperthermostability simply by introducing seven thermostabilizing residues from the extreme N-terminus of TfxA. This work suggested that mutations in the extreme N-terminus were sufficient for the mesophilic xylanase SoxB to acquire hyperthermostability.
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