Visualization of Cellulases and Cellulose Degradation

Author(s):  
Alan R. White
Author(s):  
Déborah Aires Almeida ◽  
Maria Augusta Crivelente Horta ◽  
Jaire Alves Ferreira Filho ◽  
Natália Faraj Murad ◽  
Anete Pereira de Souza

2010 ◽  
Vol 192 (24) ◽  
pp. 6492-6493 ◽  
Author(s):  
Angel Angelov ◽  
Susanne Liebl ◽  
Meike Ballschmiter ◽  
Mechthild Bömeke ◽  
Rüdiger Lehmann ◽  
...  

ABSTRACT Spirochaeta thermophila is a thermophilic, free-living anaerobe that is able to degrade various α- and β-linked sugar polymers, including cellulose. We report here the complete genome sequence of S. thermophila DSM 6192, which is the first genome sequence of a thermophilic, free-living member of the Spirochaetes phylum. The genome data reveal a high density of genes encoding enzymes from more than 30 glycoside hydrolase families, a noncellulosomal enzyme system for (hemi)cellulose degradation, and indicate the presence of a novel carbohydrate-binding module.


TECHNOLOGY ◽  
2015 ◽  
Vol 03 (02n03) ◽  
pp. 80-83
Author(s):  
Mark Polikovsky ◽  
Eshel Ben-Jacob ◽  
Alin Finkelshtein

Cellulose hydrolysis has many industrial applications such as biofuel production, food, paper and textile manufacture. Here, we present a novel approach to cellulose hydrolysis using a consortium of motile bacteria, Paenibacillus vortex, that can swarm on solid medium carrying a non-motile recombinant E. coli cargo strain expressing the β-glucosidase and cellulase genes that facilitate the hydrolysis of cellulose. These two species cooperate; the relationship is mutually beneficial: the E. coli is dispersed over long distances, while the P. vortex bacteria gain from the supply of cellulose degradation products. This enables the use of such consortia in this area of biotechnology.


2012 ◽  
Vol 76 (8) ◽  
pp. 3401-3410 ◽  
Author(s):  
M. Felipe-Sotelo ◽  
J. Hinchliff ◽  
N. Evans ◽  
P. Warwick ◽  
D. Read

AbstractThe sorption behaviour of I−, Cs+, Ni2+, Eu3+, Th4+ and UO2+2on NRVB (Nirex reference vault backfill) a possible vault backfill, at pH 12.8 was studied. Sorption isotherms generated were compared to results obtained in the presence of cellulose degradation products (CDP). Whereas Cs was not affected by the presence of the organic compounds, a notable reduction in the sorption of Th and Eu to cement was observed. The results also indicated limited removal of Ni from solution (with or without an organic ligand) by sorption, the concentration in solution seemingly being determined solely by solubility processes. In the case of uranium, the presence of CDP increased the sorption to cement by almost one order of magnitude. Further studies into the uptake of CDP by cement are being undertaken to identify the mechanism(s) responsible.


1980 ◽  
Vol 26 (7) ◽  
pp. 760-765 ◽  
Author(s):  
J. N. Saddler ◽  
A. W. Khan

Acetivibrio cellulolyticus, an isolate from an established sewage sludge culture, degraded cellulose powder, Avicel cellulose, and cellobiose. The organism showed maximum cellulose degradation in a medium containing 10 g/L of cellulose and it could also degrade cellulose in media containing up to 75 g/L of cellulose. During the exponential growth phase, large quantities of cellulolytic enzymes were found extracellularly whereas cellobiase activity was cell associated. The crude culture supernate contained endo- and exo-glucanase activities with a pH optimum at 5.0 and a temperature optimum at 50 °C. Maximum cellulase activities were detected in 2- to 3-day-old cultures grown on 1 g/L of cellulose. Cellulose concentration above 10 g/L caused the adsorption of these enzymes to the substrate and consequently lowered their detection in the supernate. The activities at 50 °C for endoglucanase, exoglucanase, and filter paper degrading ability, expressed as micrograms of glucose equivalents released per minute per milligram of protein culture supernate, were 510, 135, and 40 respectively.


PLoS ONE ◽  
2016 ◽  
Vol 11 (11) ◽  
pp. e0165832 ◽  
Author(s):  
Isaac A. Kyeremeh ◽  
Christopher J. Charles ◽  
Simon P. Rout ◽  
Andrew P. Laws ◽  
Paul N. Humphreys

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