ArticleApplied and environmental microbiology2012
Biochemical and mutational analyses of a multidomain cellulase/mannanase from Caldicellulosiruptor bescii.
Article in Applied and environmental microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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35 citing papers in PubMed, 66 citations in OpenAlex.
- Multimodular flavobacterial enzymes specialized in coordinated decomposition of cellulose and alginate in brown algal cell walls.The ISME journal · 2026Article
- Nonspecific Binding of a Putative S-Layer Protein to Plant Cell Wall Polysaccharides-Implication for Growth Competence ofInternational journal of molecular sciences · 2025Article
- Production of cello-oligosaccharides from corncob residue by degradation-synthesis reactions.Applied microbiology and biotechnology · 2024Article
- Functional studies on tandem carbohydrate-binding modules of a multimodular enzyme possessing two catalytic domains.Applied and environmental microbiology · 2024Article
- Thermophilic β-mannanases from bacteria: production, resources, structural features and bioengineering strategies.World journal of microbiology & biotechnology · 2024Review
- Identification of WxL and S-Layer Proteins fromInternational journal of molecular sciences · 2022Article
- Impact of Modular Architecture on Activity of Glycoside Hydrolase Family 5 Subfamily 8 Mannanases.Molecules (Basel, Switzerland) · 2022Article
- Biochemical and Molecular Dynamics Study of a Novel GH 43 α-l-Arabinofuranosidase/β-Xylosidase FromFrontiers in bioengineering and biotechnology · 2022Article
- Integrated engineering of enzymes and microorganisms for improving the efficiency of industrial lignocellulose deconstruction.Engineering microbiology · 2021Review
- Unifying themes and distinct features of carbon and nitrogen assimilation by polysaccharide-degrading bacteria: a summary of four model systems.Applied microbiology and biotechnology · 2021Review
- Caldicellulosiruptor bescii Adheres to Polysaccharides via a Type IV Pilin-Dependent Mechanism.Applied and environmental microbiology · 2020Article
- Thermophilic Degradation of Hemicellulose, a Critical Feedstock in the Production of Bioenergy and Other Value-Added Products.Applied and environmental microbiology · 2020Review
- Genomic and physiological analyses reveal that extremely thermophilic Caldicellulosiruptor changbaiensis deploys uncommon cellulose attachment mechanisms.Journal of industrial microbiology & biotechnology · 2019Article
- The GH10 and GH48 dual-functional catalytic domains from a multimodular glycoside hydrolase synergize in hydrolyzing both cellulose and xylan.Biotechnology for biofuels · 2019Article
- Thermostable enzymes and polysaccharides produced by thermophilic bacteria isolated from Bulgarian hot springs.Engineering in life sciences · 2018Review
- The diversity and specificity of the extracellular proteome in the cellulolytic bacteriumBiotechnology for biofuels · 2018Article
- High activity CAZyme cassette for improving biomass degradation in thermophiles.Biotechnology for biofuels · 2018Article
- Functional Analysis of the Glucan Degradation Locus in Caldicellulosiruptor bescii Reveals Essential Roles of Component Glycoside Hydrolases in Plant Biomass Deconstruction.Applied and environmental microbiology · 2017Article
- Insights into the roles of non-catalytic residues in the active site of a GH10 xylanase with activity on cellulose.The Journal of biological chemistry · 2017Article
- Oxidation of a non-phenolic lignin model compound by twoBiotechnology for biofuels · 2017Article
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3 authors at 2 institutions in 1 country.
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Abstract
Thermophilic cellulases and hemicellulases are of significant interest to the biofuel industry due to their perceived advantages over their mesophilic counterparts. We describe here biochemical and mutational analyses of Caldicellulosiruptor bescii Cel9B/Man5A (CbCel9B/Man5A), a highly thermophilic enzyme. As one of the highly secreted proteins of C. bescii, the enzyme is likely to be critical to nutrient acquisition by the bacterium. CbCel9B/Man5A is a modular protein composed of three carbohydrate-binding modules flanked at the N terminus and the C terminus by a glycoside hydrolase family 9 (GH9) module and a GH5 module, respectively. Based on truncational analysis of the polypeptide, the cellulase and mannanase activities within CbCel9B/Man5A were assigned to the N- and C-terminal modules, respectively. CbCel9B/Man5A and its truncational mutants, in general, exhibited a pH optimum of ∼5.5 and a temperature optimum of 85°C. However, at this temperature, thermostability was very low. After 24 h of incubation at 75°C, the wild-type protein maintained 43% activity, whereas a truncated mutant, TM1, maintained 75% activity. The catalytic efficiency with phosphoric acid swollen cellulose as a substrate for the wild-type protein was 7.2 s(-1) ml/mg, and deleting the GH5 module led to a mutant (TM1) with a 2-fold increase in this kinetic parameter. Deletion of the GH9 module also increased the apparent k(cat) of the truncated mutant TM5 on several mannan-based substrates; however, a concomitant increase in the K(m) led to a decrease in the catalytic efficiencies on all substrates. These observations lead us to postulate that the two catalytic activities are coupled in the polypeptide.
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