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.

scholarly journals Genome Sequence of the Polysaccharide-Degrading, Thermophilic Anaerobe Spirochaeta thermophila DSM 6192

2010 ◽  
Vol 192 (24) ◽  
pp. 6492-6493 ◽  
Author(s):  
Angel Angelov ◽  
Susanne Liebl ◽  
Meike Ballschmiter ◽  
Mechthild Bömeke ◽  
Rüdiger Lehmann ◽  
...  
Keyword(s):  
Genome Sequence ◽  
Complete Genome Sequence ◽  
Glycoside Hydrolase ◽  
Enzyme System ◽  
Cellulose Degradation ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Module ◽  
Free Living ◽  
Genome Data ◽  
Genes Encoding

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.

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

scholarly journals Characterization of Paenibacillus curdlanolyticus B-6 Xyn10D, a Xylanase That Contains a Family 3 Carbohydrate-Binding Module

2011 ◽  
Vol 77 (12) ◽  
pp. 4260-4263 ◽  
Author(s):  
Makiko Sakka ◽  
Yurika Higashi ◽  
Tetsuya Kimura ◽  
Khanok Ratanakhanokchai ◽  
Kazuo Sakka
Keyword(s):  
Recombinant Proteins ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Module ◽  
Content Type ◽  
Paenibacillus Curdlanolyticus ◽  
Biochemical Analyses ◽  
Hydrolysis Of

ABSTRACTPaenibacillus curdlanolyticusB-6 Xyn10D is a xylanase containing a family 3 carbohydrate-binding module (CBM3). Biochemical analyses using recombinant proteins derived from Xyn10D suggested that the CBM3 polypeptide has an affinity for cellulose and xylan and that CBM3 in Xyn10D is important for hydrolysis of insoluble arabinoxylan and natural biomass.

scholarly journals CalkGH9T: A Glycoside Hydrolase Family 9 Enzyme from Clostridium alkalicellulosi

Catalysts ◽  
2021 ◽  
Vol 11 (8) ◽  
pp. 1011
Author(s):  
Paripok Phitsuwan ◽  
Sengthong Lee ◽  
Techly San ◽  
Khanok Ratanakhanokchai
Keyword(s):  
Glycoside Hydrolase ◽  
Cellulose Degradation ◽  
Glycoside Hydrolase Family ◽  
Carbohydrate Binding ◽  
Type I ◽  
Amorphous Cellulose ◽  
Carbohydrate Binding Modules ◽  
Glycoside Hydrolase Family 9 ◽  
Hydrolysis Of ◽  
Hydrolase Family

Glycoside hydrolase family 9 (GH9) endoglucanases are important enzymes for cellulose degradation. However, their activity on cellulose is diverse. Here, we cloned and expressed one GH9 enzyme (CalkGH9T) from Clostridium alkalicellulosi in Escherichia coli. CalkGH9T has a modular structure, containing one GH9 catalytic module, two family 3 carbohydrate binding modules, and one type I dockerin domain. CalkGH9T exhibited maximal activity at pH 7.0–8.0 and 55 °C and was resistant to urea and NaCl. It efficiently hydrolyzed carboxymethyl cellulose (CMC) but poorly degraded regenerated amorphous cellulose (RAC). Despite strongly binding to Avicel, CalkGH9T lacked the ability to hydrolyze this substrate. The hydrolysis of CMC by CalkGH9T produced a series of cello-oligomers, with cellotetraose being preferentially released. Similar proportions of soluble and insoluble reducing ends generated by hydrolysis of RAC indicated non-processive activity. Our study extends our knowledge of the molecular mechanism of cellulose hydrolysis by GH9 family endoglucanases with industrial relevance.

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 Properties of a family 56 carbohydrate-binding module and its role in the recognition and hydrolysis of β-1,3-glucan

2017 ◽  
Vol 292 (41) ◽  
pp. 16955-16968 ◽  
Author(s):  
Andrew Hettle ◽  
Alexander Fillo ◽  
Kento Abe ◽  
Patricia Massel ◽  
Benjamin Pluvinage ◽  
...  
Keyword(s):  
Carbohydrate Binding ◽  
Carbohydrate Binding Module ◽  
Hydrolysis Of
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