scholarly journals Oxidized Cellulose Binding to Allergens with a Carbohydrate-Binding Module Attenuates Allergic Reactions

2010 ◽  
Vol 186 (2) ◽  
pp. 1240-1247 ◽  
Author(s):  
Nir Shani ◽  
Ziv Shani ◽  
Oded Shoseyov ◽  
Rufayda Mruwat ◽  
David Shoseyov
Keyword(s):  
Carbohydrate Binding ◽  
Allergic Reactions ◽  
Carbohydrate Binding Module ◽  
Oxidized Cellulose ◽  
Cellulose Binding

scholarly journals A Single Mutation in the Carbohydrate-Binding Module Enhances Cellulase Activity in Bacillus Amyloliquefaciens Mutant

2021 ◽  
Vol 18 (18) ◽  
Author(s):  
Nitipol POLSA ◽  
Chomphunuch SONGSIRIRITTHIGUL ◽  
Wasana SUYOTHA ◽  
Sugunya SUEBSAN ◽  
Somboon ANUNTALABHOCHAI ◽  
...  
Keyword(s):  
Amino Acid ◽  
Bacillus Amyloliquefaciens ◽  
Cellulase Activity ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Module ◽  
Single Mutation ◽  
Plasma Technology ◽  
Lignocellulosic Wastes ◽  
Cellulose Binding ◽  
Hydrolysis Activity

From our earlier work, we modified the carbohydrate-binding module (CBM) of Bacillus amyloliquefaciens to increase cellulase activity using cold plasma technology. The cellulase gene (BglC-M) from the mutant was expressed in Escherichia coli BL21(DE3) under the T7 promoter. The hydrolysis activity of the cellulase mutant (BglC-M) was approximately 2.5-fold higher than the control (BglC-W) over a wide range of pH and temperature conditions. The amino acid sequence of the mutant BglC-M contained 471 residues that were almost identical to the control BglC-W. Only a single amino acid, lysine, was replaced by glutamic acid at position 370 (K370E) within the carbohydrate-binding module (CBM). Structure prediction and substrate docking of BglC-M indicated that the single mutation (K370E) might involve cellulose binding of the β-sandwich facilitated by hydrogen bonding. The docking study of cellopentaose with the model structure of BglC-M indicated that the replacement of lysine-370 led to the formation of a hydrogen bond with 436Y, which has a shorter distance (2.6 Å) compared with the control (5.4 Å). As a result, the structure becomes more compact and stable, resulting in increased catalytic efficiency. Finally, the biomass hydrolysis ability of cellulase was investigated on lignocellulosic wastes such as pineapple peel, corncob, and durian peel. The BglC-M enzyme showed a more significant amount of reducing sugar released from all lignocellulosic wastes than the control. This was the first evidence that altering the base composition of the cellulose binding module enhanced the catalytic activity. HIGHLIGHTS Increasing cellulase activity of Bacillus amyloliquefaciens using plasma technology Mutation at cellulose-binding module enhance cellulase hydrolysis activity Greater cellulase activity in the hydrolysis on lignocellulosic wastes GRAPHICAL ABSTRACT

scholarly journals Extra tyrosine in the carbohydrate-binding module ofIrpex lacteusXyn10B enhances its cellulose-binding ability

2015 ◽  
Vol 79 (5) ◽  
pp. 738-746 ◽  
Author(s):  
Hiroto Nishijima ◽  
Kouichi Nozaki ◽  
Masahiro Mizuno ◽  
Tsutomu Arai ◽  
Yoshihiko Amano
Keyword(s):  
Carbohydrate Binding ◽  
Carbohydrate Binding Module ◽  
Binding Ability ◽  
Cellulose Binding

scholarly journals A mannanase, ManA, of the polycentric anaerobic fungusOrpinomycessp. strain PC-2 has carbohydrate binding and docking modules

2005 ◽  
Vol 51 (7) ◽  
pp. 559-568 ◽  
Author(s):  
Eduardo A Ximenes ◽  
Huizhong Chen ◽  
Irina A Kataeva ◽  
Michael A Cotta ◽  
Carlos R Felix ◽  
...  
Keyword(s):  
Specific Activity ◽  
High Specific Activity ◽  
Glycoside Hydrolases ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Module ◽  
Amino Acid Residues ◽  
Anaerobic Fungus ◽  
Ph Profile ◽  
Catalytic Module ◽  
Cellulose Binding

The anaerobic fungus Orpinomyces sp. strain PC-2 produces a broad spectrum of glycoside hydrolases, most of which are components of a high molecular mass cellulosomal complex. Here we report about a cDNA (manA) having 1924 bp isolated from the fungus and found to encode a polypeptide of 579 amino acid residues. Analysis of the deduced sequence revealed that it had a mannanase catalytic module, a family 1 carbohydrate-binding module, and a noncatalytic docking module. The catalytic module was homologous to aerobic fungal mannanases belonging to family 5 glycoside hydrolases, but unrelated to the previously isolated mannanases (family 26) of the anaerobic fungus Piromyces. No mannanase activity could be detected in Escherichia coli harboring a manA-containing plasmid. The manA was expressed in Saccharomyces cerevisiae and ManA was secreted into the culture medium in multiple forms. The purified extracellular heterologous mannanase hydrolyzed several types of mannan but lacked activity against cellulose, chitin, or β-glucan. The enzyme had high specific activity toward locust bean mannan and an extremely broad pH profile. It was stable for several hours at 50 °C, but was rapidly inactivated at 60 °C. The carbohydrate-binding module of the Man A produced separately in E. coli bound preferably to insoluble lignocellulosic substrates, suggesting that it might play an important role in the complex enzyme system of the fungus for lignocellulose degradation.Key words: Orpinomyces, anaerobic fungi, mannanase, cellulose-binding module, cellulosome.

scholarly journals Recognition of xyloglucan by the crystalline cellulose-binding site of a family 3a carbohydrate-binding module

FEBS Letters ◽  
2015 ◽  
Vol 589 (18) ◽  
pp. 2297-2303 ◽  
Author(s):  
Mercedes C. Hernandez-Gomez ◽  
Maja G. Rydahl ◽  
Artur Rogowski ◽  
Carl Morland ◽  
Alan Cartmell ◽  
...  
Keyword(s):  
Binding Site ◽  
Crystalline Cellulose ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Module ◽  
Cellulose Binding

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.

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