scholarly journals Effect of Glycosylation and Additional Domains on the Thermostability of a Family 10 Xylanase Produced by Thermopolyspora flexuosa

2009 ◽  
Vol 76 (1) ◽  
pp. 356-360 ◽  
Author(s):  
Sasikala Anbarasan ◽  
Janne Jänis ◽  
Marja Paloheimo ◽  
Mikko Laitaoja ◽  
Minna Vuolanto ◽  
...  
Keyword(s):  
Structural Features ◽  
Low Ph ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Module ◽  
Slight Effect ◽  
Family 10 Xylanase

ABSTRACT The effects of different structural features on the thermostability of Thermopolyspora flexuosa xylanase XYN10A were investigated. A C-terminal carbohydrate binding module had only a slight effect, whereas a polyhistidine tag increased the thermostability of XYN10A xylanase. In contrast, glycosylation at Asn26, located in an exposed loop, decreased the thermostability of the xylanase. The presence of a substrate increased stability mainly at low pH.

scholarly journals Novel Endotype Xanthanase from Xanthan-DegradingMicrobacteriumsp. Strain XT11

2018 ◽  
Vol 85 (2) ◽  
Author(s):  
Fan Yang ◽  
He Li ◽  
Jie Sun ◽  
Xiaoyu Guo ◽  
Xinyu Zhang ◽  
...  
Keyword(s):  
Catalytic Domain ◽  
Degradation Mechanism ◽  
Gel Permeation Chromatography ◽  
Structural Features ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Module ◽  
Chromatography Analysis ◽  
Shear Dependent Viscosity ◽  
Aqueous Conditions ◽  
Dependent Viscosity

ABSTRACTUnder general aqueous conditions, xanthan appears in an ordered conformation, which makes its backbone largely resistant to degradation by known cellulases. Therefore, the xanthan degradation mechanism is still unclear because of the lack of an efficient hydrolase. Here, we report the catalytic properties of MiXen, a xanthan-degrading enzyme identified from the genusMicrobacterium. MiXen is a 952-amino-acid protein that is unique to strain XT11. Both the sequence and structural features suggested that MiXen belongs to a new branch of the GH9 family and has a multimodular structure in which a catalytic (α/α)6barrel is flanked by an N-terminal Ig-like domain and by a C-terminal domain that has very few homologues in sequence databases and functions as a carbohydrate-binding module (CBM). Based on circular dichroism, shear-dependent viscosity, and reducing sugar and gel permeation chromatography analysis, we demonstrated that recombinant MiXen efficiently and randomly cleaved glucosidic bonds within the highly ordered xanthan substrate. A MiXen mutant free of the C-terminal CBM domain partially lost its xanthan-hydrolyzing ability because of decreased affinity toward xanthan, indicating the CBM domain assisted MiXen in hydrolyzing highly ordered xanthan via recognizing and binding to the substrate. Furthermore, side chain substituents and the terminal mannosyl residue significantly influenced the activity of MiXen via the formation of barriers to enzymolysis. Overall, the results of this study provide insight into the hydrolysis mechanism and enzymatic properties of a novel endotype xanthanase that will benefit future applications.IMPORTANCEThis work characterized a novel endotype xanthanase, MiXen, and elucidated that the C-terminal carbohydrate-binding module of MiXen could drastically enhance the hydrolysis activity of the enzyme toward highly ordered xanthan. Both the sequence and structural analysis demonstrated that the catalytic domain and carbohydrate-binding module of MiXen belong to the novel branch of the GH9 family and CBMs, respectively. This xanthan cleaver can help further reveal the enzymolysis mechanism of xanthan and provide an efficient tool for the production of molecular modified xanthan with new physicochemical and physiological functions.

scholarly journals O-glycosylation effects on family 1 carbohydrate-binding module solution structures

FEBS Journal ◽  
2015 ◽  
Vol 282 (22) ◽  
pp. 4341-4356 ◽  
Author(s):  
Renee M. Happs ◽  
Xiaoyang Guan ◽  
Michael G. Resch ◽  
Mark F. Davis ◽  
Gregg T. Beckham ◽  
...  
Keyword(s):  
Carbohydrate Binding ◽  
Carbohydrate Binding Module ◽  
Solution Structures

The N-terminal family 22 carbohydrate-binding module of xylanase 10B ofClostridium themocellumis not a thermostabilizing domain

2004 ◽  
Vol 238 (1) ◽  
pp. 71-78
Author(s):  
Fernando M.V. Dias ◽  
Arun Goyal ◽  
Harry J. Gilbert ◽  
José A.M. Prates ◽  
Luís M.A. Ferreira ◽  
...  
Keyword(s):  
Carbohydrate Binding ◽  
Carbohydrate Binding Module

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.

Systematic Docking Study of the Carbohydrate Binding Module Protein of Cel7A with the Cellulose Iα Crystal Model

2010 ◽  
Vol 114 (1) ◽  
pp. 49-58 ◽  
Author(s):  
Toshifumi Yui ◽  
Hirohide Shiiba ◽  
Yuya Tsutsumi ◽  
Sachio Hayashi ◽  
Tatsuhiko Miyata ◽  
...  
Keyword(s):  
Docking Study ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Module ◽  
Cellulose Iα ◽  
Crystal Model

scholarly journals N-Glycosidase–carbohydrate-binding module fusion proteins as immobilized enzymes for protein deglycosylation

2005 ◽  
Vol 18 (10) ◽  
pp. 497-501 ◽  
Author(s):  
Emily M. Kwan ◽  
Alisdair B. Boraston ◽  
Bradley W. McLean ◽  
Douglas G. Kilburn ◽  
R. Antony J. Warren
Keyword(s):  
Fusion Proteins ◽  
Immobilized Enzymes ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Module

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.

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