Study and design of stability in GH5 cellulases
Thermostable enzymes that hydrolyze lignocellulosic materials provide potential
advantages in process configuration and enhancement of production efficiency over their …
advantages in process configuration and enhancement of production efficiency over their …
A novel thermostable cellulase cocktail enhances lignocellulosic bioconversion and biorefining in a broad range of pH
Lignocellulose is the most abundant biomass in nature, and the effective biorefining of them
is dependent upon enzymes with high catalytic activity and stability in extreme pH and high …
is dependent upon enzymes with high catalytic activity and stability in extreme pH and high …
Purification and characterisation of alkaline cellulase produced by a novel isolate, Bacillus sphaericus JS1
A novel strain of Bacillus sphaericus JS1 producing thermostable alkaline carboxymethyl
cellulase (CMCase; endo-1, 4-β-glucanase, EC 3.2. 1.4) was isolated from soil using …
cellulase (CMCase; endo-1, 4-β-glucanase, EC 3.2. 1.4) was isolated from soil using …
Optimization, Purification, and Characterization of Extracellular Mesophilic Alkaline Cellulase from Sponge-Associated Marinobacter sp. MSI032
Abstract Marinobacter sp.(MSI032) isolated from the marine sponge Dendrilla nigra was
optimized for the production of extracellular cellulolytic enzyme (CMCase) by submerged …
optimized for the production of extracellular cellulolytic enzyme (CMCase) by submerged …
A highly thermostable crude endoglucanase produced by a newly isolated Thermobifida fusca strain UPMC 901
MHM Zainudin, NA Mustapha, MA Hassan… - Scientific Reports, 2019 - nature.com
A thermophilic Thermobifida fusca strain UPMC 901, harboring highly thermostable
cellulolytic activity, was successfully isolated from oil palm empty fruit bunch compost. Its …
cellulolytic activity, was successfully isolated from oil palm empty fruit bunch compost. Its …
Optimization of carboxymethylcellulase production from Bacillus amyloliquefaciens SS35
In this paper, we have attempted optimization of production of enzyme
carboxymethylcellulase or endoglucanase from the bacterium Bacillus amyloliquefaciens …
carboxymethylcellulase or endoglucanase from the bacterium Bacillus amyloliquefaciens …
[PDF][PDF] A new halo-alkaliphilic, thermostable endoglucanase from moderately halophilic Bacillus sp. C14 isolated from Van soda lake
A Aygan, B Arikan - Int J Agric Biol, 2008 - researchgate.net
Bacillus sp. C14 isolated from Van Soda Lake, Turkey, produced halo-alkaliphilic
endoglucanase at 37ºC at pH 9. Analyses of the enzyme for molecular mass and cellulolytic …
endoglucanase at 37ºC at pH 9. Analyses of the enzyme for molecular mass and cellulolytic …
Alkaline thermostable and halophilic endoglucanase from Bacillus licheniformis C108
A Aygan, L Karcioglu, B Arikan - African Journal of Biotechnology, 2011 - ajol.info
An endoglucanase was purified from halophilic alkaline Bacillus licheniformis isolated from
soils of Lake Van in Turkey. The optimal pH and temperature of the endoglucanase …
soils of Lake Van in Turkey. The optimal pH and temperature of the endoglucanase …
A novel thermostable and halostable carboxymethylcellulase from marine bacterium Bacillus licheniformisAU01
N Annamalai, R Thavasi, S Vijayalakshmi… - World Journal of …, 2011 - Springer
A novel thermostable, halostable carboxymethylcellulase (CMCase) from a marine
bacterium Bacillus licheniformis AU01 was purified 10.4-fold with 18% yield with a specific …
bacterium Bacillus licheniformis AU01 was purified 10.4-fold with 18% yield with a specific …
Utilization of renewable agricultural residues for the production of extracellular halostable cellulase from newly isolated Halomonas sp. strain PS47
P Shivanand, G Mugeraya, A Kumar - Annals of microbiology, 2013 - Springer
A newly isolated biopolymer-degrading halophilic bacterium, Halomonas sp. strain PS47,
yielded higher cellulase activity (0.0076 U/ml) in mineral salt medium (MM63). Activity …
yielded higher cellulase activity (0.0076 U/ml) in mineral salt medium (MM63). Activity …