Low temperature hydrogenolysis of waxes to diesel range gasoline and light alkanes: Comparison of catalytic properties of group 4, 5 and 6 metal hydrides supported on silica–alumina

2012 ◽  
Vol 2 (1) ◽  
pp. 215-219 ◽  
Author(s):  
Sebastien Norsic ◽  
Cherif Larabi ◽  
Marco Delgado ◽  
Anthony Garron ◽  
Aimery de Mallmann ◽  
...  
2015 ◽  
Vol 5 (10) ◽  
pp. 4765-4771 ◽  
Author(s):  
Kai C. Szeto ◽  
Nicolas Merle ◽  
Cesar Rios ◽  
Pascal Rouge ◽  
Jessica Llop Castelbou ◽  
...  

2-Butenes are transformed in a continuous flow reactor over metal hydrides of zirconium, tantalum and tungsten supported on silica–alumina. Exceptionally high selectivity to dimeric products is obtained over supported zirconium hydride catalysts.


1986 ◽  
Vol 51 (8) ◽  
pp. 1571-1578 ◽  
Author(s):  
Alois Motl

The radiation catalytic properties of the BASF K-3-10 catalyst were studied, namely the dependence of these effects on the time interval between the catalyst irradiation and the reaction itself and also on the length of the catalyst use. The catalytic effects decrease exponentially with the interval between the irradiation and the reaction if the catalyst is kept in the presence of air. The stability of effects induced by various types of radiations increases in the sequence beta radiation - gamma radiation - fast neutrons. The radiation catalytic effect stability in the reaction increases in the same sequence.


2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Ryutaro Furukawa ◽  
Wakako Toma ◽  
Koji Yamazaki ◽  
Satoshi Akanuma

Abstract Enzymes have high catalytic efficiency and low environmental impact, and are therefore potentially useful tools for various industrial processes. Crucially, however, natural enzymes do not always have the properties required for specific processes. It may be necessary, therefore, to design, engineer, and evolve enzymes with properties that are not found in natural enzymes. In particular, the creation of enzymes that are thermally stable and catalytically active at low temperature is desirable for processes involving both high and low temperatures. In the current study, we designed two ancestral sequences of 3-isopropylmalate dehydrogenase by an ancestral sequence reconstruction technique based on a phylogenetic analysis of extant homologous amino acid sequences. Genes encoding the designed sequences were artificially synthesized and expressed in Escherichia coli. The reconstructed enzymes were found to be slightly more thermally stable than the extant thermophilic homologue from Thermus thermophilus. Moreover, they had considerably higher low-temperature catalytic activity as compared with the T. thermophilus enzyme. Detailed analyses of their temperature-dependent specific activities and kinetic properties showed that the reconstructed enzymes have catalytic properties similar to those of mesophilic homologues. Collectively, our study demonstrates that ancestral sequence reconstruction can produce a thermally stable enzyme with catalytic properties adapted to low-temperature reactions.


2019 ◽  
Vol 60 (5) ◽  
pp. 492-498
Author(s):  
A. Chesalkin ◽  
A. Martaus ◽  
J. M. Averina ◽  
V. V. Men’shikov

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