The family II carbohydrate-binding module of xylanase CflXyn11A from Cellulomonas flavigena increases the synergy with cellulase TrCel7B from Trichoderma reesei during the hydrolysis of sugar cane bagasse

2012 ◽  
Vol 104 ◽  
pp. 622-630 ◽  
Author(s):  
Patricia Pavón-Orozco ◽  
Alejandro Santiago-Hernández ◽  
Anna Rosengren ◽  
María Eugenia Hidalgo-Lara ◽  
Henrik Stålbrand
Keyword(s):  
Trichoderma Reesei ◽  
Sugar Cane ◽  
Sugar Cane Bagasse ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Module ◽  
Cellulomonas Flavigena ◽  
The Family ◽  
Hydrolysis Of

scholarly journals The family 42 carbohydrate-binding module of family 54 α-L-arabinofuranosidase specifically binds the arabinofuranose side chain of hemicellulose

2006 ◽  
Vol 399 (3) ◽  
pp. 503-511 ◽  
Author(s):  
Akimasa Miyanaga ◽  
Takuya Koseki ◽  
Yozo Miwa ◽  
Yuichiro Mese ◽  
Sachiko Nakamura ◽  
...  
Keyword(s):  
Binding Pocket ◽  
Side Chain ◽  
Titration Calorimetry ◽  
Glycoside Hydrolase Family ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Module ◽  
Binding Assays ◽  
The Family ◽  
Affinity Gel Electrophoresis ◽  
Hydrolysis Of

α-L-Arabinofuranosidase catalyses the hydrolysis of the α-1,2-, α-1,3-, and α-1,5-L-arabinofuranosidic bonds in L-arabinose-containing hemicelluloses such as arabinoxylan. AkAbf54 (the glycoside hydrolase family 54 α-L-arabinofuranosidase from Aspergillus kawachii) consists of two domains, a catalytic and an arabinose-binding domain. The latter has been named AkCBM42 [family 42 CBM (carbohydrate-binding module) of AkAbf54] because homologous domains are classified into CBM family 42. In the complex between AkAbf54 and arabinofuranosyl-α-1,2-xylobiose, the arabinose moiety occupies the binding pocket of AkCBM42, whereas the xylobiose moiety is exposed to the solvent. AkCBM42 was found to facilitate the hydrolysis of insoluble arabinoxylan, because mutants at the arabinose binding site exhibited markedly decreased activity. The results of binding assays and affinity gel electrophoresis showed that AkCBM42 interacts with arabinose-substituted, but not with unsubstituted, hemicelluloses. Isothermal titration calorimetry and frontal affinity chromatography analyses showed that the association constant of AkCBM42 with the arabinose moiety is approximately 103 M−1. These results indicate that AkCBM42 binds the non-reducing-end arabinofuranosidic moiety of hemicellulose. To our knowledge, this is the first example of a CBM that can specifically recognize the side-chain monosaccharides of branched hemicelluloses.

scholarly journals On the distinct binding modes of expansin and carbohydrate-binding module proteins on crystalline and nanofibrous cellulose: implications for cellulose degradation by designer cellulosomes

2018 ◽  
Vol 20 (12) ◽  
pp. 8278-8293 ◽  
Author(s):  
Adam Orłowski ◽  
Lior Artzi ◽  
Pierre-Andre Cazade ◽  
Melissabye Gunnoo ◽  
Edward A. Bayer ◽  
...  
Keyword(s):  
Cellulose Degradation ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Module ◽  
Binding Modes ◽  
Special Group ◽  
P Transformation ◽  
Hydrolysis Of

Transformation of cellulose into monosaccharides can be achieved by hydrolysis of the cellulose chains, carried out by a special group of enzymes known as cellulases.

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

Hydrolysis of softwood by Aspergillus mannanase: Role of a carbohydrate-binding module

2010 ◽  
Vol 148 (4) ◽  
pp. 163-170 ◽  
Author(s):  
Tuan Anh Pham ◽  
Jean Guy Berrin ◽  
Eric Record ◽  
Kim Anh To ◽  
Jean-Claude Sigoillot
Keyword(s):  
Carbohydrate Binding ◽  
Carbohydrate Binding Module ◽  
Hydrolysis Of
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