ArticleScientific reports2022
Expression, characterization, and activity optimization of a novel cellulase from the thermophilic bacteria Cohnella sp. A01.
Article in Scientific reports, 2022. 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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8 citing papers in PubMed, 25 citations in OpenAlex.
- A Novel Recombinant Protein Purification Approach Using Biomolecular Condensates.International journal of molecular sciences · 2026Article
- Multi-enzyme producing lignocellulolytic bacteria from biogas slurry: molecular identification and optimization of enzyme production by Bacillus subtilis BCA-1.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2026Article
- Characterization of a novel halophilic and thermostable multifunctional cellulase from Ebinur Salt Lake.Scientific reports · 2025Article
- Statistical Modelling of Thermostable Cellulase Production Conditions of ThermophilicIndian journal of microbiology · 2024Article
- Enhanced crystalline cellulose degradation by a novel metagenome-derived cellulase enzyme.Scientific reports · 2024Article
- Biochemical and molecular characterization of novel keratinolytic protease fromFrontiers in microbiology · 2023Article
- Comparative genomic analysis ofFrontiers in microbiology · 2023Article
- Discovery of novel carbohydrate degrading enzymes from soda lakes through functional metagenomics.Frontiers in microbiology · 2022Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cellulases are hydrolytic enzymes with wide scientific and industrial applications. We described a novel cellulase, CelC307, from the thermophilic indigenous Cohnella sp. A01. The 3-D structure of the CelC307 was predicted by comparative modeling. Docking of CelC307 with specific inhibitors and molecular dynamic (MD) simulation revealed that these ligands bound in a non-competitive manner. The CelC307 protein was purified and characterized after recombinant expression in Escherichia coli (E. coli) BL21. Using CMC 1% as the substrate, the thermodynamic values were determined as K
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