ArticleInternational journal of molecular sciences2015
Cloning, Expression, and Characterization of a Thermophilic Endoglucanase, AcCel12B from Acidothermus cellulolyticus 11B.
Article in International journal of molecular sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed.
- Soil Biodiversity of Eucalyptus saligna: Insights Into Bacterial and Nematode Communities.Environmental microbiology reports · 2026Article
- Genomic and transcriptomic insights into the cellulose-degrading mechanism of Bacillus subtilis DC-11 and its novel cellulose catabolic pathway.Archives of microbiology · 2025Article
- Biochemical characterization of a bilfunctional endoglucanase/glucomannanase derived from mountain soil.Biotechnology letters · 2025Article
- Biocontrol Agents Inhibit Banana Fusarium Wilt and Alter the Rooted Soil Bacterial Community in the Field.Journal of fungi (Basel, Switzerland) · 2024Article
- Production, purification, characterization and application of two novel endoglucanases from buffalo rumen metagenome.Journal of animal science and biotechnology · 2023Article
- Changes of endophytic microbial community inFrontiers in microbiology · 2022Article
- Three glycoside hydrolase family 12 enzymes display diversity in substrate specificities and synergistic action between each other.Molecular biology reports · 2019Article
- Substrate-Related Factors Affecting Cellulosome-Induced Hydrolysis for Lignocellulose Valorization.International journal of molecular sciences · 2019Review
- A ThermostableInternational journal of molecular sciences · 2019Article
- Expression and characterisation of a thermophilic endo-1,4-β-glucanase from Sulfolobus shibatae of potential industrial application.Molecular biology reports · 2018Article
- Cellulases from Thermophiles Found by Metagenomics.Microorganisms · 2018Review
- The unique GH5 cellulase member in the extreme halotolerant fungus Aspergillus glaucus CCHA is an endoglucanase with multiple tolerance to salt, alkali and heat: prospects for straw degradation applications.Extremophiles : life under extreme conditions · 2018Article
- Finding Biomass Degrading Enzymes Through an Activity-Correlated Quantitative Proteomics Platform (ACPP).Journal of the American Society for Mass Spectrometry · 2017Article
- Article
- Cloning and expression of an endoglucanase gene from the thermotolerant fungus Aspergillus fumigatus DBiNU-1 in Kluyveromyces lactis.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology]Article
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9 authors.
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Abstract
The gene ABK52392 from the thermophilic bacterium Acidothermus cellulolyticus 11B was predicted to be endoglucanase and classified into glycoside hydrolase family 12. ABK52392 encodes a protein containing a catalytic domain and a carbohydrate binding module. ABK52392 was cloned and functionally expressed in Escherichia coli. After purification by Ni-NTA agarose affinity chromatography and Q-Sepharose® Fast Flow chromatography, the properties of the recombinant protein (AcCel12B) were characterized. AcCel12B exhibited optimal activity at pH 4.5 and 75 °C. The half-lives of AcCel12B at 60 and 70 °C were about 90 and 2 h, respectively, under acidic conditions. The specific hydrolytic activities of AcCel12B at 70 °C and pH 4.5 for sodium carboxymethylcellulose (CMC) and regenerated amorphous cellulose (RAC) were 118.3 and 104.0 U·mg(-1), respectively. The Km and Vmax of AcCel12B for CMC were 25.47 mg·mL(-1) and 131.75 U·mg(-1), respectively. The time course of hydrolysis for RAC was investigated by measuring reducing ends in the soluble and insoluble phases. The total hydrolysis rate rapidly decreased after the early stage of incubation and the generation of insoluble reducing ends decreased earlier than that of soluble reducing ends. High thermostability of the cellulase indicates its potential commercial significance and it could be exploited for industrial application in the future.
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