A thermophilic and thermostable xylanase from Caldicoprobacter algeriensis: Recombinant expression, characterization and application in paper biobleaching

2020 ◽  
Vol 164 ◽  
pp. 808-817
Author(s):  
Sonia Mhiri ◽  
Amel Bouanane-Darenfed ◽  
Sonia Jemli ◽  
Sawssan Neifar ◽  
Rihab Ameri ◽  
...  
Keyword(s):  
Recombinant Expression ◽  
Thermostable Xylanase ◽  
Expression Characterization

High Yield Recombinant Expression, Characterization and Homology Modeling of Two Types of Cis-epoxysuccinic Acid Hydrolases

2012 ◽  
Vol 31 (5) ◽  
pp. 432-438 ◽  
Author(s):  
Gu-Zhen Cui ◽  
Shan Wang ◽  
Yifei Li ◽  
Yi-Jun Tian ◽  
Yingang Feng ◽  
...  
Keyword(s):  
Homology Modeling ◽  
Recombinant Expression ◽  
High Yield ◽  
Acid Hydrolases ◽  
Expression Characterization

Recombinant expression, characterization, and pulp prebleaching property of a Phanerochaete chrysosporium endo-β-1,4-mannanase

2007 ◽  
Vol 41 (6-7) ◽  
pp. 740-747 ◽  
Author(s):  
Regis-Olivier Benech ◽  
Xiaoming Li ◽  
Donald Patton ◽  
Justin Powlowski ◽  
Reginald Storms ◽  
...  
Keyword(s):  
Phanerochaete Chrysosporium ◽  
Recombinant Expression ◽  
Expression Characterization

Recombinant expression, characterization, and application of a phospholipase B from Fusarium oxysporum

2017 ◽  
Vol 242 ◽  
pp. 92-100 ◽  
Author(s):  
Lingqia Su ◽  
Dening Ji ◽  
Xiumei Tao ◽  
Lingang Yu ◽  
Jing Wu ◽  
...  
Keyword(s):  
Fusarium Oxysporum ◽  
Recombinant Expression ◽  
Phospholipase B ◽  
Expression Characterization

scholarly journals Recombinant expression, characterization and phylogenetic studies of novels cystatins-like proteins of sweet orange (Citrus sinensis) and clementine (Citrus clementina)

2020 ◽  
Vol 152 ◽  
pp. 546-553 ◽  
Author(s):  
Vanessa Karine Schneider ◽  
Taíse Fernanda da Silva Ferrara ◽  
Sâmara Vieira Rocha ◽  
Célio Dias Santos-Júnior ◽  
Daniela Morilha Neo-Justino ◽  
...  
Keyword(s):  
Citrus Sinensis ◽  
Sweet Orange ◽  
Recombinant Expression ◽  
Citrus Clementina ◽  
Phylogenetic Studies ◽  
Expression Characterization

scholarly journals Gene Cloning, Recombinant Expression, Characterization, and Molecular Modeling of the Glycolytic Enzyme Triosephosphate Isomerase from Fusarium oxysporum

2019 ◽  
Vol 8 (1) ◽  
pp. 40 ◽  
Author(s):  
Beatriz Hernández-Ochoa ◽  
Saúl Gómez-Manzo ◽  
Erick Alcaraz-Carmona ◽  
Hugo Serrano-Posada ◽  
Sara Centeno-Leija ◽  
...  
Keyword(s):  
Active Site ◽  
Triosephosphate Isomerase ◽  
Recombinant Expression ◽  
Glycolytic Enzyme ◽  
Kinetic Characteristics ◽  
Structural Determinants ◽  
Future Studies ◽  
Optimal Activity ◽  
Expression Characterization ◽  
Potential Use

Triosephosphate isomerase (TPI) is a glycolysis enzyme, which catalyzes the reversible isomerization between dihydroxyactetone-3-phosphate (DHAP) and glyceraldehyde-3-phosphate (GAP). In pathogenic organisms, TPI is essential to obtain the energy used to survive and infect. Fusarium oxisporum (Fox) is a fungus of biotechnological importance due to its pathogenicity in different organisms, that is why the relevance of also biochemically analyzing its TPI, being the first report of its kind in a Fusarium. Moreover, the kinetic characteristics or structural determinants related to its function remain unknown. Here, the Tpi gene from F. oxysporum was isolated, cloned, and overexpressed. The recombinant protein named FoxTPI was purified (97% purity) showing a molecular mass of 27 kDa, with optimal activity at pH 8.0 and and temperature of 37 °C. The values obtained for Km and Vmax using the substrate GAP were 0.47 ± 0.1 mM, and 5331 μmol min−1 mg−1, respectively. Furthemore, a protein structural modeling showed that FoxTPI has the classical topology of TPIs conserved in other organisms, including the catalytic residues conserved in the active site (Lys12, His94 and Glu164). Finally, when FoxTPI was analyzed with inhibitors, it was found that one of them inhibits its activity, which gives us the perspective of future studies and its potential use against this pathogen.

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