ArticleAMB Express2020
Cloning and characterization of low-temperature adapted GH5-CBM3 endo-cellulase from Bacillus subtilis 1AJ3 and their application in the saccharification of switchgrass and coffee grounds.
Article in AMB Express, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Engineering of multiple modules to enhance lignocellulose degradation ability inSynthetic and systems biotechnology · 2026Article
- Discovery and functional characterization of endoglucanases fromApplied and environmental microbiology · 2026Article
- Genomic architecture and transcriptional regulation of cellulose degradation in the novel marine bacterium Pseudoxanthomonas sp. JC1303.Molecular genetics and genomics : MGG · 2026Article
- Characterization of a novel halophilic and thermostable multifunctional cellulase from Ebinur Salt Lake.Scientific reports · 2025Article
- Apoplastic proteomic reveals Colletotrichum fructicola effector CfXyn11A recognized by tobacco and suppressed by pear in the apoplast.Molecular horticulture · 2025Article
- Introduction of Cellulolytic BacteriumMicroorganisms · 2024Article
- Enhanced crystalline cellulose degradation by a novel metagenome-derived cellulase enzyme.Scientific reports · 2024Article
- The effects of different doses of compound enzyme preparations on the production performance, meat quality and rumen microorganisms of yak were studied by metagenomics and transcriptomics.Frontiers in microbiology · 2024Article
- Biochemical Characterization of Novel GH6 Endoglucanase fromFoods (Basel, Switzerland) · 2023Article
- Degradation of switchgrass byFrontiers in microbiology · 2022Article
- Characterization of a GH8 β-1,4-Glucanase fromJournal of microbiology and biotechnology · 2021Article
- Industrial applications of cold-adapted enzymes: challenges, innovations and future perspective.3 Biotech · 2021Review
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8 authors.
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Abstract
Endocellulase is a key cellulase for cellulosic material pretreatment in the industry by hydrolyzing long cellulose chains into short chains. To investigate the endocellulase characteristics from Bacillus subtilis 1AJ3, and increase its production yield, this paper cloned an endocellulase gene denoted CEL-5A from strain 1AJ3 and expressed in E. coli BL21 (DE3). The CEL-5A gene was sequenced with a full-length of 1500 bp, encoding a totally of 500 amino acids, and containing two domains: the GH5 family catalytic domain (CD) and the CBM3 family cellulose-binding domain (CBD). Recombinant endocellulase Cel-5A with a His-tag was purified of the Ni-NTA column, and SDS-PAGE results demonstrated that Cel-5A exhibited a molecular weight of 56.4 kDa. The maximum enzyme activity of Cel-5A was observed at pH 4.5 and 50 °C. Moreover, it was active over the broad temperature region of 30-60 °C, and stable within the pH range of 4.5-10.0. In addition, Co
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