scholarly journals Reduced type‐A carbohydrate‐binding module interactions to cellulose I leads to improved endocellulase activity

2020 ◽  
Author(s):  
Bhargava Nemmaru ◽  
Nicholas Ramirez ◽  
Cindy J. Farino ◽  
John M. Yarbrough ◽  
Nicholas Kravchenko ◽  
...  
Keyword(s):  
Type A ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Module ◽  
Cellulose I

Comparative Analysis of Crystallinity Changes in Cellulose I Polymers Using ATR-FTIR, X-ray Diffraction, and Carbohydrate-Binding Module Probes

2011 ◽  
Vol 12 (11) ◽  
pp. 4121-4126 ◽  
Author(s):  
Alenka Kljun ◽  
Thomas A. S. Benians ◽  
Florence Goubet ◽  
Frank Meulewaeter ◽  
J. Paul Knox ◽  
...  
Keyword(s):  
Comparative Analysis ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Module ◽  
X Ray Diffraction ◽  
Cellulose I ◽  
X Ray ◽  
Crystallinity Changes

scholarly journals Reduced Type-A Carbohydrate-Binding Module Interactions to Cellulose Leads to Improved Endocellulase Activity

2020 ◽  
Author(s):  
Bhargava Nemmaru ◽  
Nicholas Ramirez ◽  
Cindy J. Farino ◽  
John M. Yarbrough ◽  
Nicholas Kravchenko ◽  
...  
Keyword(s):  
Type A ◽  
Cellulose Hydrolysis ◽  
Cellulolytic Enzymes ◽  
Carbohydrate Binding ◽  
Binding Assays ◽  
Cellulose I ◽  
Enzyme Binding ◽  
Equilibrium Binding ◽  
Hydrolysis Activity

AbstractDissociation of non-productively bound cellulolytic enzymes from cellulose is hypothesized to be a key rate-limiting factor impeding cost-effective biomass conversion to fermentable sugars. However, the role of carbohydrate-binding modules (CBMs) in enabling non-productive enzyme binding is not well understood. Here, we examine the subtle interplay of CBM binding and cellulose hydrolysis activity for three model Type-A CBMs (families 1, 3a, and 64) tethered to a multifunctional endoglucanase (CelE) on two distinct cellulose allomorphs (i.e., cellulose I and III). We generated a small-library of mutant CBMs with varying cellulose affinity, as determined by equilibrium binding assays, followed by monitoring cellulose hydrolysis activity of CelE-CBM fusion constructs. Finally, kinetic binding assays using quartz crystal microbalance with dissipation (QCM-D) were employed to measure CBM adsorption and desorption rate constants Kon and Koff, respectively, towards nanocrystalline cellulose derived from both allomorphs. Overall, our results indicate that reduced CBM equilibrium binding affinity towards cellulose I alone, resulting from increased desorption rates (Koff) and reduced effective adsorption rates (nKon), is correlated to overall improved endocellulase activity. Future studies could employ similar approaches to unravel the role of CBMs in non-productive enzyme binding and develop improved cellulolytic enzymes for industrial applications.

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
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