Bimetallic solvated metal atom dispersed catalysts. New materials with low-temperature catalytic properties

1984 ◽  
Vol 106 (9) ◽  
pp. 2721-2722 ◽  
Author(s):  
Kenneth J. Klabunde ◽  
Yuzo Imizu
Keyword(s):  
Low Temperature ◽  
Metal Atom ◽  
Catalytic Properties ◽  
New Materials ◽  
Dispersed Catalysts

Effect of the ionizing radiation on the catalytic activity of the BASF K-3-10 catalyst in the low-temperature conversion of carbon monoxide by water vapour. Stability of the radiation catalytic effects

1986 ◽  
Vol 51 (8) ◽  
pp. 1571-1578 ◽  
Author(s):  
Alois Motl
Keyword(s):  
Carbon Monoxide ◽  
Catalytic Activity ◽  
Low Temperature ◽  
Catalytic Effect ◽  
Catalytic Properties ◽  
Beta Radiation ◽  
Fast Neutrons ◽  
Time Interval ◽  
The Stability ◽  
Catalytic Effects

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.

scholarly journals Ancestral sequence reconstruction produces thermally stable enzymes with mesophilic enzyme-like catalytic properties

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Ryutaro Furukawa ◽  
Wakako Toma ◽  
Koji Yamazaki ◽  
Satoshi Akanuma
Keyword(s):  
Low Temperature ◽  
Catalytic Properties ◽  
Amino Acid Sequences ◽  
Ancestral Sequence ◽  
Kinetic Properties ◽  
Reconstruction Technique ◽  
Thermally Stable ◽  
Ancestral Sequence Reconstruction ◽  
Ancestral Sequences ◽  
Sequence Reconstruction

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.

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