Exemplar Abstract for Caldicellulosiruptor bescii Yang et al. 2010.

2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
Kara Mannor ◽  
George M Garrity
Keyword(s):  
Caldicellulosiruptor Bescii

scholarly journals Metabolic engineering of Caldicellulosiruptor bescii yields increased hydrogen production from lignocellulosic biomass

2013 ◽  
Vol 6 (1) ◽  
pp. 85 ◽  
Author(s):  
Minseok Cha ◽  
Daehwan Chung ◽  
James G Elkins ◽  
Adam M Guss ◽  
Janet Westpheling
Keyword(s):  
Metabolic Engineering ◽  
Hydrogen Production ◽  
Lignocellulosic Biomass ◽  
Caldicellulosiruptor Bescii

scholarly journals Engineering redox-balanced ethanol production in the cellulolytic and extremely thermophilic bacterium, Caldicellulosiruptor bescii

2018 ◽  
Vol 7 ◽  
pp. e00073 ◽  
Author(s):  
Amanda M. Williams-Rhaesa ◽  
Gabriel M. Rubinstein ◽  
Israel M. Scott ◽  
Gina L. Lipscomb ◽  
Farris L. Poole, II ◽  
...  
Keyword(s):  
Ethanol Production ◽  
Thermophilic Bacterium ◽  
Caldicellulosiruptor Bescii

scholarly journals The thermophilic biomass-degrading bacterium Caldicellulosiruptor bescii utilizes two enzymes to oxidize glyceraldehyde 3-phosphate during glycolysis

2019 ◽  
Vol 294 (25) ◽  
pp. 9995-10005 ◽  
Author(s):  
Israel M. Scott ◽  
Gabriel M. Rubinstein ◽  
Farris L. Poole ◽  
Gina L. Lipscomb ◽  
Gerrit J. Schut ◽  
...  
Keyword(s):  
Large Subunit ◽  
Small Subunit ◽  
Lag Phase ◽  
Cellulolytic Bacterium ◽  
Ferredoxin Oxidoreductase ◽  
Caldicellulosiruptor Bescii ◽  
Degrading Bacterium ◽  
Growth Optimum ◽  
Cell Densities ◽  
Aldehyde Ferredoxin Oxidoreductase

Caldicellulosiruptor bescii is an extremely thermophilic, cellulolytic bacterium with a growth optimum at 78 °C and is the most thermophilic cellulose degrader known. It is an attractive target for biotechnological applications, but metabolic engineering will require an in-depth understanding of its primary pathways. A previous analysis of its genome uncovered evidence that C. bescii may have a completely uncharacterized aspect to its redox metabolism, involving a tungsten-containing oxidoreductase of unknown function. Herein, we purified and characterized this new member of the aldehyde ferredoxin oxidoreductase family of tungstoenzymes. We show that it is a heterodimeric glyceraldehyde-3-phosphate (GAP) ferredoxin oxidoreductase (GOR) present not only in all known Caldicellulosiruptor species, but also in 44 mostly anaerobic bacterial genera. GOR is phylogenetically distinct from the monomeric GAP-oxidizing enzyme found previously in several Archaea. We found that its large subunit (GOR-L) contains a single tungstopterin site and one iron-sulfur [4Fe-4S] cluster, that the small subunit (GOR-S) contains four [4Fe-4S] clusters, and that GOR uses ferredoxin as an electron acceptor. Deletion of either subunit resulted in a distinct growth phenotype on both C5 and C6 sugars, with an increased lag phase, but higher cell densities. Using metabolomics and kinetic analyses, we show that GOR functions in parallel with the conventional GAP dehydrogenase, providing an alternative ferredoxin-dependent glycolytic pathway. These two pathways likely facilitate the recycling of reduced redox carriers (NADH and ferredoxin) in response to environmental H2 concentrations. This metabolic flexibility has important implications for the future engineering of this and related species.

scholarly journals A Novel Glucose Isomerase from Caldicellulosiruptor bescii with Great Potentials in the Production of High-Fructose Corn Syrup

2020 ◽  
Vol 2020 ◽  
pp. 1-7
Author(s):  
Chenxia Dai ◽  
Tingting Miao ◽  
Jinping Hai ◽  
Yunyi Xiao ◽  
Ying Li ◽  
...  
Keyword(s):  
Catalytic Efficiency ◽  
Cost Effective ◽  
Glucose Isomerase ◽  
Substrate Affinity ◽  
High Fructose Corn Syrup ◽  
Industrial Enzymes ◽  
Corn Syrup ◽  
Caldicellulosiruptor Bescii ◽  
High Fructose ◽  
The Cost

Glucose isomerase (GI) that catalyzes the conversion of D-glucose to D-fructose is one of the most important industrial enzymes for the production of high-fructose corn syrup (HFCS). In this study, a novel GI (CbGI) was cloned from Caldicellulosiruptor bescii and expressed in Escherichia coli. The purified recombinant CbGI (rCbGI) showed neutral and thermophilic properties. It had optimal activities at pH 7.0 and 80°C and retained stability at 85°C. In comparison with other reported GIs, rCbGI exhibited higher substrate affinity (Km=42.61 mM) and greater conversion efficiency (up to 57.3% with 3M D-glucose as the substrate). The high catalytic efficiency and affinity of this CbGI is much valuable for the cost-effective production of HFCS.

scholarly journals Enzymatic Biotransformation of Balloon Flower Root Saponins into Bioactive Platycodin D by Deglucosylation with Caldicellulosiruptor bescii β-Glucosidase

2019 ◽  
Vol 20 (16) ◽  
pp. 3854 ◽  
Author(s):  
Tae-Geun Kil ◽  
Su-Hwan Kang ◽  
Tae-Hun Kim ◽  
Kyung-Chul Shin ◽  
Deok-Kun Oh
Keyword(s):  
Pharmacological Activity ◽  
Plant Root ◽  
Industrial Applications ◽  
The Other ◽  
Root Extract ◽  
Reaction Conditions ◽  
Platycodin D ◽  
Caldicellulosiruptor Bescii ◽  
Platycodi Radix ◽  
Biotransformation Process

Platycodin D (PD), a major saponin (platycoside) in Platycodi radix (balloon flower root), has higher pharmacological activity than the other major platycosides; however, its content in the plant root is only approximately 10% (w/w) and the productivities of PD by several enzymes are still too low for industrial applications. To rapidly increase the total PD content, the β-glucosidase from Caldicellulosiruptor bescii was used for the deglucosylation of the PD precursors platycoside E (PE) and platycodin D3 (PD3) in the root extract into PD. Under the optimized reaction conditions, the enzyme completely converted the PD precursors into PD with the highest productivity reported so far, increasing the total PD content to 48% (w/w). In the biotransformation process, the platycosides in Platycodi radix were hydrolyzed by four pathways: deapiosylated (deapi)-PE → deapi-PD3 → deapi-PD, PE → PD3 → PD, polygalacin D3 → polygalacin D, and 3″-O-acetyl polygalacin D3 → 3″-O-acetyl polygalacin D.

scholarly journals Molecular and Biochemical Analyses of the GH44 Module of CbMan5B/Cel44A, a Bifunctional Enzyme from the Hyperthermophilic Bacterium Caldicellulosiruptor bescii

2012 ◽  
Vol 78 (19) ◽  
pp. 7048-7059 ◽  
Author(s):  
Libin Ye ◽  
Xiaoyun Su ◽  
George E. Schmitz ◽  
Young Hwan Moon ◽  
Jing Zhang ◽  
...  
Keyword(s):  
Specific Activity ◽  
Cellulose Hydrolysis ◽  
Thermophilic Bacterium ◽  
Carbohydrate Binding ◽  
Content Type ◽  
Caldicellulosiruptor Bescii ◽  
C Terminus ◽  
Carbohydrate Binding Modules ◽  
Β Sheets ◽  
Biochemical Analyses

ABSTRACTA large polypeptide encoded in the genome of the thermophilic bacteriumCaldicellulosiruptor besciiwas determined to consist of two glycoside hydrolase (GH) modules separated by two carbohydrate-binding modules (CBMs). Based on the detection of mannanase and endoglucanase activities in the N-terminal GH5 and the C-terminal GH44 module, respectively, the protein was designated CbMan5B/Cel44A. A GH5 module with >99% identity from the same organism was characterized previously (X. Su, R. I. Mackie, and I. K. Cann, Appl. Environ. Microbiol.78:2230-2240, 2012); therefore, attention was focused on CbMan5A/Cel44A-TM2 (or TM2), which harbors the GH44 module and the two CBMs. On cellulosic substrates, TM2 had an optimal temperature and pH of 85°C and 5.0, respectively. Although the amino acid sequence of the GH44 module of TM2 was similar to those of other GH44 modules that hydrolyzed cello-oligosaccharides, cellulose, lichenan, and xyloglucan, it was unique that TM2 also displayed modest activity on mannose-configured substrates and xylan. The TM2 protein also degraded Avicel with higher specific activity than activities reported for its homologs. The GH44 catalytic module is composed of a TIM-like domain and a β-sandwich domain, which consists of one β-sheet at the N terminus and nine β-sheets at the C terminus. Deletion of one or more β-sheets from the β-sandwich domain resulted in insoluble proteins, suggesting that the β-sandwich domain is essential for proper folding of the polypeptide. Combining TM2 with three other endoglucanases fromC. besciiled to modest synergistic activities during degradation of cellulose, and based on our results, we propose a model for cellulose hydrolysis and utilization byC. bescii.

Sign in / Sign up

Export Citation Format

Share Document