Cellulose Binding Domain Increases Cellulose Synthase Activity in Acetobacter Xylinum, and Biomass of Transgenic Plants

1999 ◽  
pp. 213-218 ◽  
Author(s):  
Ziv Shani ◽  
Etai Shpigel ◽  
Levava Roiz ◽  
Raphael Goren ◽  
Basia Vinocur ◽  
...  
Keyword(s):  
Transgenic Plants ◽  
Cellulose Synthase ◽  
Acetobacter Xylinum ◽  
Binding Domain ◽  
Cellulose Binding Domain ◽  
Cellulose Binding

scholarly journals Cellulose as an inert matrix for presenting cytokines to target cells: production and properties of a stem cell factor–cellulose-binding domain fusion protein

1999 ◽  
Vol 339 (2) ◽  
pp. 429-434
Author(s):  
J. Greg DOHENY ◽  
Eric J. JERVIS ◽  
M. Marta GUARNA ◽  
R. Keith HUMPHRIES ◽  
R. Antony J. WARREN ◽  
...  
Keyword(s):  
Stem Cell ◽  
Fusion Protein ◽  
Stem Cell Factor ◽  
Direct Analysis ◽  
Binding Domain ◽  
Target Cells ◽  
Cellulose Binding Domain ◽  
Binding Characteristics ◽  
Cellulose Binding ◽  
Cellulose Surface

A chimaera of stem cell factor (SCF) and a cellulose-binding domain from the xylanase Cex (CBDCex) effectively immobilizes SCF on a cellulose surface. The fusion protein retains both the cytokine properties of SCF and the cellulose-binding characteristics of CBDCex. When adsorbed on cellulose, SCF–CBDCex is up to 7-fold more potent than soluble SCF–CBDCex and than native SCF at stimulating the proliferation of factor-dependent cell lines. When cells are incubated with cellulose-bound SCF–CBDCex, activated receptors and SCF–CBDCex co-localize on the cellulose matrix. The strong binding of SCF–CBDCex to the cellulose surface permits the effective and localized stimulation of target cells; this is potentially significant for long-term perfusion culturing of factor-dependent cells. It also permits the direct analysis of the effects of surface-bound cytokines on target cells.

scholarly journals Fusion Endoglucanase Cel12B from Thermotoga maritima with Cellulose Binding Domain

BioResources ◽  
2018 ◽  
Vol 13 (2) ◽  
Author(s):  
Hao Shi ◽  
Yanling Chen ◽  
Wenjian Peng ◽  
Pixiang Wang ◽  
Yuping Zhao ◽  
...  
Keyword(s):  
Thermotoga Maritima ◽  
Binding Domain ◽  
Cellulose Binding Domain ◽  
Cellulose Binding

scholarly journals Acetyl xylan esterase II fromPenicillium purpurogenumis similar to an esterase fromTrichoderma reeseibut lacks a cellulose binding domain

FEBS Letters ◽  
1998 ◽  
Vol 423 (1) ◽  
pp. 35-38 ◽  
Author(s):  
Rodrigo Gutiérrez ◽  
Ella Cederlund ◽  
Lars Hjelmqvist ◽  
Alessandra Peirano ◽  
Francisco Herrera ◽  
...  
Keyword(s):  
Binding Domain ◽  
Cellulose Binding Domain ◽  
Acetyl Xylan Esterase ◽  
Cellulose Binding

Fabrication of cotton fabrics using family III cellulose-binding domain for enhanced surface properties

RSC Advances ◽  
2016 ◽  
Vol 6 (107) ◽  
pp. 105202-105205 ◽  
Author(s):  
Liting Zhang ◽  
Yaofei Sun ◽  
Wenji Yao ◽  
Guoying Dai ◽  
Ping Wang
Keyword(s):  
Surface Properties ◽  
Cotton Fabric ◽  
Surface Functionalization ◽  
Physical Adsorption ◽  
Cotton Fabrics ◽  
Binding Domain ◽  
Cellulose Binding Domain ◽  
Fabric Surface ◽  
Cellulose Binding ◽  
Enhanced Surface

Cotton fabric surface functionalization by physical adsorption of CBDIII through a sample soaking process.

scholarly journals Probing the role of tryptophan residues in a cellulose-binding domain by chemical modification

1996 ◽  
Vol 5 (11) ◽  
pp. 2311-2318 ◽  
Author(s):  
Mark R. Bray ◽  
Neil R. Gilkes ◽  
Douglas G. Kilburn ◽  
R. Antony J. Warren ◽  
Lawrence P. Mcintosh ◽  
...  
Keyword(s):  
Chemical Modification ◽  
Binding Domain ◽  
Cellulose Binding Domain ◽  
Tryptophan Residues ◽  
Cellulose Binding

scholarly journals Properties and Mutation Analysis of the CelK Cellulose-Binding Domain from the Clostridium thermocellum Cellulosome

2001 ◽  
Vol 183 (5) ◽  
pp. 1552-1559 ◽  
Author(s):  
Irina A. Kataeva ◽  
Ronald D. Seidel ◽  
Xin-Liang Li ◽  
Lars G. Ljungdahl
Keyword(s):  
Amino Acids ◽  
Calcium Binding ◽  
Clostridium Thermocellum ◽  
Binding Capacity ◽  
Binding Domain ◽  
Cellulose Binding Domain ◽  
Calcium Binding Site ◽  
Aromatic Residues ◽  
Cellulose Binding ◽  
Family Iv

ABSTRACT The family IV cellulose-binding domain of Clostridium thermocellum CelK (CBDCelK) was expressed inEscherichia coli and purified. It binds to acid-swollen cellulose (ASC) and bacterial microcrystalline cellulose (BMCC) with capacities of 16.03 and 3.95 μmol/g of cellulose and relative affinities (K r) of 2.33 and 9.87 liters/g, respectively. The CBDCelK is the first representative of family IV CBDs to exhibit an affinity for BMCC. The CBDCelKalso binds to the soluble polysaccharides lichenin, glucomannan, and barley β-glucan, which are substrates for CelK. It does not bind to xylan, galactomannan, and carboxymethyl cellulose. The CBDCelK contains 1 mol of calcium per mol. The CBDCelK has three thiol groups and one disulfide, reduction of which results in total loss of cellulose-binding ability. To reveal amino acid residues important for biological function of the domain and to investigate the role of calcium in the CBDCelK four highly conserved aromatic residues (Trp56, Trp94, Tyr111, and Tyr136) and Asp192 were mutated into alanines, giving the mutants W56A, W94A, Y111A, Y136A, and D192A. In addition 14 N-terminal amino acids were deleted, giving the CBD-NCelK. The CBD-NCelK and D192A retained binding parameters close to that of the intact CBDCelK, W56A and W94A totally lost the ability to bind to cellulose, Y136A bound to both ASC and BMCC but with significantly reduced binding capacity and K rand Y111A bound weakly to ASC and did not bind to BMCC. Mutations of the aromatic residues in the CBDCelK led to structural changes revealed by studying solubility, circular-dichroism spectra, dimer formation, and aggregation. Calcium content was drastically decreased in D192A. The results suggest that Asp192 is in the calcium-binding site of the CBDCelK and that calcium does not affect binding to cellulose. The 14 amino acids from the N terminus of the CBDCelK are not important for binding. Tyr136, corresponding to Cellulomonas fimi CenC CBDN1Y85, located near the binding cleft, might be involved in the formation of the binding surface, while Y111, W56A, and W94A are essential for the binding process by keeping the CBDCelK correctly folded.

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