scholarly journals Oxygen nonstoichiometry and thermodynamic characterization of Zr doped ceria in the 1573–1773 K temperature range

2015 ◽  
Vol 17 (12) ◽  
pp. 7813-7822 ◽  
Author(s):  
M. Takacs ◽  
J. R. Scheffe ◽  
A. Steinfeld

The thermodynamics and defect chemistry of Zr4+-doped ceria is investigated and discussed in regards to the efficiency of solar thermochemical redox cycles.

2018 ◽  
Vol 20 (34) ◽  
pp. 22099-22113 ◽  
Author(s):  
Matthias Grünbacher ◽  
Lukas Schlicker ◽  
Maged F. Bekheet ◽  
Aleksander Gurlo ◽  
Bernhard Klötzer ◽  
...  

Acceptor doping of CeO2 substantially influences defect chemistry, bulk structure, hydrogen solubility and hydroxyl chemistry in hydrogen atmospheres.


Author(s):  
Beatrix Huber ◽  
Klaus W. Richter ◽  
Hans Flandorfer ◽  
Adolf Mikula ◽  
Herbert Ipser

2020 ◽  
Vol 65 (5) ◽  
pp. 747-751
Author(s):  
S. V. Sysoev ◽  
T. M. Kuzin ◽  
L. N. Zelenina ◽  
K. V. Zherikova ◽  
N. V. Gelfond

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Saleem Farooq ◽  
Ruqeya Nazir ◽  
Shabir Ahmad Ganai ◽  
Bashir Ahmad Ganai

AbstractAs an approach to the exploration of cold-active enzymes, in this study, we isolated a cold-active protease produced by psychrotrophic bacteria from glacial soils of Thajwas Glacier, Himalayas. The isolated strain BO1, identified as Bacillus pumilus, grew well within a temperature range of 4–30 °C. After its qualitative and quantitative screening, the cold-active protease (Apr-BO1) was purified. The Apr-BO1 had a molecular mass of 38 kDa and showed maximum (37.02 U/mg) specific activity at 20 °C, with casein as substrate. It was stable and active between the temperature range of 5–35 °C and pH 6.0–12.0, with an optimum temperature of 20 °C at pH 9.0. The Apr-BO1 had low Km value of 1.0 mg/ml and Vmax 10.0 µmol/ml/min. Moreover, it displayed better tolerance to organic solvents, surfactants, metal ions and reducing agents than most alkaline proteases. The results exhibited that it effectively removed the stains even in a cold wash and could be considered a decent detergent additive. Furthermore, through protein modelling, the structure of this protease was generated from template, subtilisin E of Bacillus subtilis (PDB ID: 3WHI), and different methods checked its quality. For the first time, this study reported the protein sequence for psychrotrophic Apr-BO1 and brought forth its novelty among other cold-active proteases.


2005 ◽  
Vol 14 (9) ◽  
pp. 2387-2404 ◽  
Author(s):  
María C. Lidón-Moya ◽  
Francisco N. Barrera ◽  
Marta Bueno ◽  
Raúl Pérez-Jiménez ◽  
Javier Sancho ◽  
...  

2009 ◽  
Vol 89 (3-4) ◽  
pp. 257-267 ◽  
Author(s):  
Latha-Selvi Canabady-Rochelle ◽  
Christian Sanchez ◽  
Michel Mellema ◽  
Sylvie Banon

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