ArticleApplied and environmental microbiology2015
Distinct roles for carbohydrate-binding modules of glycoside hydrolase 10 (GH10) and GH11 xylanases from Caldicellulosiruptor sp. strain F32 in thermostability and catalytic efficiency.
Article in Applied and environmental microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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27 citing papers in PubMed, 64 citations in OpenAlex.
- Biochemical and structural characterization of AmyY fromApplied and environmental microbiology · 2026Article
- Characterization of the thermophilic xylanase Fsa02490Xyn from the hyperthermophile Fervidibacter sacchari belonging to glycoside hydrolase family 10.FEBS open bio · 2025Article
- Genome-Wide Identification and Analysis of Carbohydrate-Binding Modules inInternational journal of molecular sciences · 2025Article
- Functional studies on tandem carbohydrate-binding modules of a multimodular enzyme possessing two catalytic domains.Applied and environmental microbiology · 2024Article
- Research progress of multi-enzyme complexes based on the design of scaffold protein.Bioresources and bioprocessing · 2023Review
- Biochemical and Regulatory Analyses of Xylanolytic Regulons in Caldicellulosiruptor bescii Reveal Genus-Wide Features of Hemicellulose Utilization.Applied and environmental microbiology · 2022Article
- Enhancement of catalytic activity and alkaline stability of cellobiohydrolase by structure-based protein engineering.3 Biotech · 2022Article
- Effects of Module Truncation of a New Alginate Lyase VxAly7C from MarineInternational journal of molecular sciences · 2022Article
- Toward Microbial Recycling and Upcycling of Plastics: Prospects and Challenges.Frontiers in microbiology · 2022Review
- A thermostable and CBM2-linked GH10 xylanase fromFrontiers in bioengineering and biotechnology · 2022Article
- Improving the Thermostability of a Fungal GH11 Xylanase via Fusion of a Submodule (C2) from Hyperthermophilic CBM9_1-2.International journal of molecular sciences · 2021Article
- The Role of Glycoside Hydrolases in Phytopathogenic Fungi and Oomycetes Virulence.International journal of molecular sciences · 2021Review
- Preparation of β(1→3)/β(1→4) xylooligosaccharides from red alga dulse by two xylanases from Streptomyces thermogriseus.Bioresources and bioprocessing · 2021Article
- Carbohydrate-binding modules targeting branched polysaccharides: overcoming side-chain recalcitrance in a non-catalytic approach.Bioresources and bioprocessing · 2021Review
- Tryptic Mapping Based Structural Insights of Endo-1, 4-β-Xylanase fromIndian journal of microbiology · 2020Article
- Effects of oligolignol sizes and binding modes on a GH11 xylanase inhibition revealed by molecular modeling techniques.Journal of molecular modeling · 2020Article
- The biology and biotechnology of the genus Caldicellulosiruptor: recent developments in 'Caldi World'.Extremophiles : life under extreme conditions · 2020Review
- Heterologous expression and functional characterization of a GH10 endoxylanase fromBiotechnology reports (Amsterdam, Netherlands) · 2019Article
- Genomic and physiological analyses reveal that extremely thermophilic Caldicellulosiruptor changbaiensis deploys uncommon cellulose attachment mechanisms.Journal of industrial microbiology & biotechnology · 2019Article
- Comparative Biochemical and Structural Analysis of Novel Cellulose Binding Proteins (Tāpirins) from Extremely ThermophilicApplied and environmental microbiology · 2019Article
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7 authors at 4 institutions in 1 country.
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Abstract
Xylanases are crucial for lignocellulosic biomass deconstruction and generally contain noncatalytic carbohydrate-binding modules (CBMs) accessing recalcitrant polymers. Understanding how multimodular enzymes assemble can benefit protein engineering by aiming at accommodating various environmental conditions. Two multimodular xylanases, XynA and XynB, which belong to glycoside hydrolase families 11 (GH11) and GH10, respectively, have been identified from Caldicellulosiruptor sp. strain F32. In this study, both xylanases and their truncated mutants were overexpressed in Escherichia coli, purified, and characterized. GH11 XynATM1 lacking CBM exhibited a considerable improvement in specific activity (215.8 U nmol(-1) versus 94.7 U nmol(-1)) and thermal stability (half-life of 48 h versus 5.5 h at 75°C) compared with those of XynA. However, GH10 XynB showed higher enzyme activity and thermostability than its truncated mutant without CBM. Site-directed mutagenesis of N-terminal amino acids resulted in a mutant, XynATM1-M, with 50% residual activity improvement at 75°C for 48 h, revealing that the disordered region influenced protein thermostability negatively. The thermal stability of both xylanases and their truncated mutants were consistent with their melting temperature (Tm), which was determined by using differential scanning calorimetry. Through homology modeling and cross-linking analysis, we demonstrated that for XynB, the resistance against thermoinactivation generally was enhanced through improving both domain properties and interdomain interactions, whereas for XynA, no interdomain interactions were observed. Optimized intramolecular interactions can accelerate thermostability, which provided microbes a powerful evolutionary strategy to assemble catalysts that are adapted to various ecological conditions.
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