scholarly journals Purification and Characterization of Thermostable Cellulase from Consortium XM70 in Terrestrial Hot Spring with Sugarcane Bagasse

2015 ◽  
Vol 14 (4) ◽  
pp. 591 ◽  
Author(s):  
C Zhao ◽  
X Lu ◽  
Y Deng ◽  
Y Huang ◽  
B Liu
Keyword(s):  
Sugarcane Bagasse ◽  
Hot Spring ◽  
Purification And Characterization ◽  
Thermostable Cellulase ◽  
Terrestrial Hot Spring

Characterization of Microaerobacter geothermalis gen. nov., sp. nov., a novel microaerophilic, nitrate- and nitrite-reducing thermophilic bacterium isolated from a terrestrial hot spring in Tunisia

Extremophiles ◽  
2010 ◽  
Vol 14 (3) ◽  
pp. 297-304 ◽  
Author(s):  
Nadia Khelifi ◽  
Emna Ben Romdhane ◽  
Abdeljabbar Hedi ◽  
Anne Postec ◽  
Marie-Laure Fardeau ◽  
...  
Keyword(s):  
Hot Spring ◽  
Thermophilic Bacterium ◽  
Nitrate And Nitrite ◽  
Terrestrial Hot Spring

Purification and characterization of a thermostable cellulase-free xylanase from the newly isolated Paecilomyces themophila

2006 ◽  
Vol 38 (6) ◽  
pp. 780-787 ◽  
Author(s):  
Lite Li ◽  
Hongmei Tian ◽  
Yongqiang Cheng ◽  
Zhengqiang Jiang ◽  
Shaoqing Yang
Keyword(s):  
Purification And Characterization ◽  
Thermostable Cellulase

Purification and characterization of thermostable cellulase from Enterobacter cloacae IP8 isolated from decayed plant leaf litter

2017 ◽  
Vol 35 (5) ◽  
pp. 379-387 ◽  
Author(s):  
Abayomi Isaac Akintola ◽  
Olaoluwa Oyedeji ◽  
Mufutau Kolawole Bakare ◽  
Isaac Olusanjo Adewale
Keyword(s):  
Leaf Litter ◽  
Enterobacter Cloacae ◽  
Purification And Characterization ◽  
Plant Leaf ◽  
Thermostable Cellulase

scholarly journals Purification and Characterization of a New Thermostable, Haloalkaline, Solvent Stable, and Detergent Compatible Serine Protease fromGeobacillus toebiiStrain LBT 77

2016 ◽  
Vol 2016 ◽  
pp. 1-8 ◽  
Author(s):  
Wajdi Thebti ◽  
Yosra Riahi ◽  
Omrane Belhadj
Keyword(s):  
Serine Protease ◽  
Hot Spring ◽  
Deae Cellulose ◽  
Ammonium Sulfate Precipitation ◽  
Purification And Characterization ◽  
Optimum Ph ◽  
High Concentrations ◽  
First Time ◽  
Solvent Stable

A new thermostable, haloalkaline, solvent stable SDS-induced serine protease was purified and characterized from a thermophilicGeobacillus toebiiLBT 77 newly isolated from a Tunisian hot spring. This study reveals the potential of the protease fromGeobacillus toebiiLBT 77 as an additive to detergent with spectacular proprieties described for the first time. The protease was purified to homogeneity by ammonium sulfate precipitation followed by Sephadex G-75 and DEAE-Cellulose chromatography. It was a monomeric enzyme with molecular weight of 30 kDa. The optimum pH, temperature, and NaCl for maximum protease activity were 13.0, 95°C, and 30%, respectively. Activity was stimulated by Ca2+, Mg2+, DTNB,β-mercaptoethanol, and SDS. The protease was extremely stable even at pH 13.25, 90°C, and 30% NaCl and in the presence of hydrophilic, hydrophobic solvents at high concentrations. The high compatibility with ionic, nonionic, and commercial detergents confirms the utility as an additive to cleaning products. Kinetic and thermodynamic characterization of protease revealedKm=1 mg mL−1,  Vmax=217.5 U mL−1,Kcat/Km=99 mg mL−1 S−1,Ea=51.5 kJ mol−1, andΔG⁎=56.5 kJ mol−1.

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