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
- 0000 0004 1936 738X grid.213876.9 Department of Genetics University of Georgia 30602 Athens GA USA, 0000 0001 0789 9563 grid.254224.7 Department of Food Science and Technology Chung-Ang University 17546 Anseong Gyeonggi Republic of Korea, 0000 0004 0446 2659 grid.135519.a The BioEnergy Science Center and the Center for BioEnergy Innovation Oak Ridge National Laboratory 37831 Oak Ridge TN USA
- 0000 0001 2199 3636 grid.419357.d Biosciences Center, National Renewable Energy Laboratory Golden CO USA, 0000 0004 0446 2659 grid.135519.a The BioEnergy Science Center and the Center for BioEnergy Innovation Oak Ridge National Laboratory 37831 Oak Ridge TN USA
- 0000 0004 1936 738X grid.213876.9 Department of Genetics University of Georgia 30602 Athens GA USA, 0000 0004 0446 2659 grid.135519.a The BioEnergy Science Center and the Center for BioEnergy Innovation Oak Ridge National Laboratory 37831 Oak Ridge TN USA
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. besciii 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.
- Research Organization:
- National Renewable Energy Laboratory (NREL), Golden, CO (United States)
- Sponsoring Organization:
- USDOE Office of Science (SC), Biological and Environmental Research (BER)
- Grant/Contract Number:
- AC05-00OR22725; AC36-08GO28308
- OSTI ID:
- 1772499
- Alternate ID(s):
- OSTI ID: 1505928
- Report Number(s):
- NREL/JA-2700-73412
- Journal Information:
- Journal of Industrial Microbiology and Biotechnology, Journal Name: Journal of Industrial Microbiology and Biotechnology Vol. 46 Journal Issue: 5; ISSN 1367-5435
- Publisher:
- Oxford University PressCopyright Statement
- Country of Publication:
- Germany
- Language:
- English
Web of Science
Genomic and physiological analyses reveal that extremely thermophilic Caldicellulosiruptor changbaiensis deploys uncommon cellulose attachment mechanisms
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journal | August 2019 |
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In vivo synergistic activity of a CAZyme cassette from Acidothermus cellulolyticus significantly improves the cellulolytic activity of the C. bescii exoproteome
Expression of a Cellobiose Phosphorylase from Thermotoga maritima in Caldicellulosiruptor bescii Improves the Phosphorolytic Pathway and Results in a Dramatic Increase in Cellulolytic Activity