ArticlePloS one2013
Structure and function of a novel cellulase 5 from sugarcane soil metagenome.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 72 citations in OpenAlex.
- Enhanced crystalline cellulose degradation by a novel metagenome-derived cellulase enzyme.Scientific reports · 2024Article
- Discovery, structural characterization, and functional insights into a novel apiosidase from the GH140 family, isolated from a lignocellulolytic-enriched mangrove microbial community.Biotechnology letters · 2024Article
- Soil microbiome engineering for sustainability in a changing environment.Nature biotechnology · 2023Review
- Biochemical and structural characterisation of a family GH5 cellulase from endosymbiont of shipworm P. megotara.Biotechnology for biofuels and bioproducts · 2023Article
- Role of metagenomics in prospecting novel endoglucanases, accentuating functional metagenomics approach in second-generation biofuel production: a review.Biomass conversion and biorefinery · 2023Review
- In silico characterization of the GH5-cellulase family from uncultured microorganisms: physicochemical and structural studies.Journal, genetic engineering & biotechnology · 2021Article
- Cellulases: From Bioactivity to a Variety of Industrial Applications.Biomimetics (Basel, Switzerland) · 2021Review
- A snapshot of microbial diversity and function in an undisturbed sugarcane bagasse pile.BMC biotechnology · 2020Article
- Cellulolytic thermophilic microorganisms in white biotechnology: a review.Folia microbiologica · 2020Review
- A processive endoglucanase with multi-substrate specificity is characterized from porcine gut microbiota.Scientific reports · 2019Article
- A Novel Subfamily of Endo-β-1,4-Glucanases in Glycoside Hydrolase Family 10.Applied and environmental microbiology · 2019Article
- Biochemical Characterization of a Novel Monospecific Endo-β-1,4-Glucanase Belonging to GH Family 5 From a Rhizosphere Metagenomic Library.Frontiers in microbiology · 2019Article
- Cellulases from Thermophiles Found by Metagenomics.Microorganisms · 2018Review
- Diversity of Microbial Carbohydrate-Active enZYmes (CAZYmes) Associated with Freshwater and Soil Samples from Caatinga Biome.Microbial ecology · 2017Article
- Functional and structural characterization of a novel putative cysteine protease cell wall-modifying multi-domain enzyme selected from a microbial metagenome.Scientific reports · 2016Article
- A Novel Carbohydrate-binding Module from Sugar Cane Soil Metagenome Featuring Unique Structural and Carbohydrate Affinity Properties.The Journal of biological chemistry · 2016Article
- Bifunctional recombinant cellulase-xylanase (rBhcell-xyl) from the polyextremophilic bacterium Bacillus halodurans TSLV1 and its utility in valorization of renewable agro-residues.Extremophiles : life under extreme conditions · 2016Article
- Chemical stability of a cold-active cellulase with high tolerance toward surfactants and chaotropic agent.Biotechnology reports (Amsterdam, Netherlands) · 2016Article
- Discovery and Characterization of a Thermostable and Highly Halotolerant GH5 Cellulase from an Icelandic Hot Spring Isolate.PloS one · 2016Article
- Cloning, purification, crystallization and preliminary X-ray studies of a carbohydrate-binding module from family 64 (StX).Acta crystallographica. Section F, Structural biology communications · 2015Article
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Authors and funding
12 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cellulases play a key role in enzymatic routes for degradation of plant cell-wall polysaccharides into simple and economically-relevant sugars. However, their low performance on complex substrates and reduced stability under industrial conditions remain the main obstacle for the large-scale production of cellulose-derived products and biofuels. Thus, in this study a novel cellulase with unusual catalytic properties from sugarcane soil metagenome (CelE1) was isolated and characterized. The polypeptide deduced from the celE1 gene encodes a unique glycoside hydrolase domain belonging to GH5 family. The recombinant enzyme was active on both carboxymethyl cellulose and β-glucan with an endo-acting mode according to capillary electrophoretic analysis of cleavage products. CelE1 showed optimum hydrolytic activity at pH 7.0 and 50 °C with remarkable activity at alkaline conditions that is attractive for industrial applications in which conventional acidic cellulases are not suitable. Moreover, its three-dimensional structure was determined at 1.8 Å resolution that allowed the identification of an insertion of eight residues in the β8-α8 loop of the catalytic domain of CelE1, which is not conserved in its psychrophilic orthologs. This 8-residue-long segment is a prominent and distinguishing feature of thermotolerant cellulases 5 suggesting that it might be involved with thermal stability. Based on its unconventional characteristics, CelE1 could be potentially employed in biotechnological processes that require thermotolerant and alkaline cellulases.
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