scholarly journals Molecular basis for the preferential recognition of β1,3‐1,4‐glucans by the family 11 carbohydrate‐binding module from Clostridium thermocellum

FEBS Journal ◽  
2019 ◽  
Vol 287 (13) ◽  
pp. 2723-2743 ◽  
Author(s):  
Diana O. Ribeiro ◽  
Aldino Viegas ◽  
Virgínia M. R. Pires ◽  
João Medeiros‐Silva ◽  
Pedro Bule ◽  
...  
Keyword(s):  
Molecular Basis ◽  
Clostridium Thermocellum ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Module ◽  
The Family ◽  
Preferential Recognition

Crystal Structures of the Family 9 Carbohydrate-Binding Module fromThermotoga maritimaXylanase 10A in Native and Ligand-Bound Forms†,‡

Biochemistry ◽  
2001 ◽  
Vol 40 (21) ◽  
pp. 6248-6256 ◽  
Author(s):  
Valerie Notenboom ◽  
Alisdair B. Boraston ◽  
Douglas G. Kilburn ◽  
David R. Rose
Keyword(s):  
Crystal Structures ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Module ◽  
The Family

Influence of positioning of carbohydrate binding module on the activity of endoglucanase CelA of Clostridium thermocellum

2012 ◽  
Vol 161 (3) ◽  
pp. 206-212 ◽  
Author(s):  
Muhammad Sajjad ◽  
M. Imran Mahmood Khan ◽  
Rehan Zafar ◽  
Sajjad Ahmad ◽  
Umar H.K. Niazi ◽  
...  
Keyword(s):  
Clostridium Thermocellum ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Module

The nature of the carbohydrate binding module determines the catalytic efficiency of xylanase Z of Clostridium thermocellum

2013 ◽  
Vol 168 (4) ◽  
pp. 403-408 ◽  
Author(s):  
Muhammad Imran M. Khan ◽  
Muhammad Sajjad ◽  
Saima Sadaf ◽  
Rehan Zafar ◽  
Umer H.K. Niazi ◽  
...  
Keyword(s):  
Clostridium Thermocellum ◽  
Catalytic Efficiency ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Module

The role of carbohydrate-binding module (CBM) repeat of a multimodular xylanase (XynX) from Clostridium thermocellum in cellulose and xylan binding

2010 ◽  
Vol 48 (6) ◽  
pp. 856-861 ◽  
Author(s):  
Thangaswamy Selvaraj ◽  
Sung Kyum Kim ◽  
Yong Ho Kim ◽  
Yu Seok Jeong ◽  
Yu-Jeong Kim ◽  
...  
Keyword(s):  
Clostridium Thermocellum ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Module

scholarly journals In VitroReconstitution of the Complete Clostridium thermocellum Cellulosome and Synergistic Activity on Crystalline Cellulose

2012 ◽  
Vol 78 (12) ◽  
pp. 4301-4307 ◽  
Author(s):  
Jan Krauss ◽  
Vladimir V. Zverlov ◽  
Wolfgang H. Schwarz
Keyword(s):  
Clostridium Thermocellum ◽  
Protein Complexes ◽  
Hydrolytic Activity ◽  
Crystalline Cellulose ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Module ◽  
Synergistic Activity ◽  
Crystalline Substrate ◽  
Culture Supernatants

ABSTRACTArtificial cellulase complexes active on crystalline cellulose were reconstitutedin vitrofrom a native mix of cellulosomal enzymes and CipA scaffoldin. Enzymes containing dockerin modules for binding to the corresponding cohesin modules were prepared from culture supernatants of aC. thermocellum cipAmutant. They were reassociated to cellulosomes via dockerin-cohesin interaction. Recombinantly produced mini-CipA proteins with one to three cohesins either with or without the carbohydrate-binding module (CBM) and the complete CipA protein were used as the cellulosomal backbone. The binding between cohesins and dockerins occurred spontaneously. The hydrolytic activity against soluble and crystalline cellulosic compounds showed that the composition of the complex does not seem to be dependent on which CipA-derived cohesin was used for reconstitution. Binding did not seem to have an obvious local preference (equal binding to Coh1 and Coh6). The synergism on crystalline cellulose increased with an increasing number of cohesins in the scaffoldin. Thein vitro-formed complex showed a 12-fold synergism on the crystalline substrate (compared to the uncomplexed components). The activity of reconstituted cellulosomes with full-size CipA reached 80% of that of native cellulosomes. Complexation on the surface of nanoparticles retained the activity of protein complexes and enhanced their stability. Partial supplementation of the native cellulosome components with three selected recombinant cellulases enhanced the activity on crystalline cellulose and reached that of the native cellulosome. This opens possibilities forin vitrocomplex reconstitution, which is an important step toward the creation of highly efficient engineered cellulases.

Sign in / Sign up

Export Citation Format

Share Document