ArticleJournal of industrial microbiology & biotechnology2019
Heterologous co-expression of two β-glucanases and a cellobiose phosphorylase resulted in a significant increase in the cellulolytic activity of the Caldicellulosiruptor bescii exoproteome.
Article in Journal of industrial microbiology & biotechnology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 11 citations in OpenAlex.
- Metabolic engineering of Caldicellulosiruptor bescii for hydrogen production.Applied microbiology and biotechnology · 2024Review
- Identification of neutral genome integration sites with high expression and high integration efficiency inSynthetic and systems biotechnology · 2023Article
- Microbial β-glucanases: production, properties, and engineering.World journal of microbiology & biotechnology · 2023Review
- Engineering Caldicellulosiruptor bescii with Surface Layer Homology Domain-Linked Glycoside Hydrolases Improves Plant Biomass Solubilization.Applied and environmental microbiology · 2022Article
- A novel SfaNI-like restriction-modification system in Caldicellulosiruptor extents the genetic engineering toolbox for this genus.PloS one · 2022Article
- Coexpression of a β-d-Xylosidase from Thermotoga maritima and a Family 10 Xylanase from Acidothermus cellulolyticus Significantly Improves the Xylan Degradation Activity of the Caldicellulosiruptor bescii Exoproteome.Applied and environmental microbiology · 2021Article
- Insights into Thermophilic Plant Biomass Hydrolysis fromMicroorganisms · 2020Review
- The biology and biotechnology of the genus Caldicellulosiruptor: recent developments in 'Caldi World'.Extremophiles : life under extreme conditions · 2020Review
- Genomic and physiological analyses reveal that extremely thermophilic Caldicellulosiruptor changbaiensis deploys uncommon cellulose attachment mechanisms.Journal of industrial microbiology & biotechnology · 2019Article
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Authors and funding
5 authors at 4 institutions in 2 countries.
Funding
Abstract
The ability to deconstruct plant biomass without conventional pretreatment has made members of the genus Caldicellulosiruptor the target of investigation for the consolidated processing of plant lignocellulosic biomass to biofuels and bioproducts. To investigate the synergy of enzymes involved and to further improve the ability of C. bescii to degrade cellulose, we introduced CAZymes that act synergistically with the C. bescii exoproteome in vivo and in vitro. We recently demonstrated that the Acidothermus cellulolyticus E1 endo-1,4-β-D-glucanase (GH5) with a family 2 carbohydrate-binding module (CBM) increased the activity of C. bescii exoproteome on biomass, presumably acting in concert with CelA. The β-glucanase, GuxA, from A. cellulolyticus is a multi-domain enzyme with strong processive exoglucanase activity, and the cellobiose phosphorylase from Thermotoga maritima catalyzes cellulose degradation acting synergistically with cellobiohydrolases and endoglucanases. We identified new chromosomal insertion sites to co-express these enzymes and the resulting strain showed a significant increase in the enzymatic activity of the exoproteome.
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