Kinetic study of ethyl octyl ether formation from ethanol and 1-octanol on Amberlyst 70

AIChE Journal ◽  
2014 ◽  
Vol 60 (8) ◽  
pp. 2918-2928 ◽  
Author(s):  
Jordi Guilera ◽  
Roger Bringué ◽  
Eliana Ramírez ◽  
Carles Fité ◽  
Javier Tejero
Keyword(s):  
Kinetic Study ◽  
Octyl Ether ◽  
Amberlyst 70

scholarly journals Kinetic study of 1-butanol dehydration to di-n-butyl ether over Amberlyst 70

AIChE Journal ◽  
2015 ◽  
Vol 62 (1) ◽  
pp. 180-194 ◽  
Author(s):  
María Ángeles Pérez-Maciá ◽  
Roger Bringué ◽  
Montserrat Iborra ◽  
Javier Tejero ◽  
Fidel Cunill
Keyword(s):  
Kinetic Study ◽  
Butyl Ether ◽  
Amberlyst 70

scholarly journals Kinetics of the liquid phase dehydration of 1‐octanol to di‐n‐octyl ether on Amberlyst 70

AIChE Journal ◽  
2017 ◽  
Vol 63 (9) ◽  
pp. 3966-3978 ◽  
Author(s):  
Carlos Casas ◽  
Roger Bringué ◽  
Carles Fité ◽  
Montserrat Iborra ◽  
Javier Tejero
Keyword(s):  
Liquid Phase ◽  
Octyl Ether ◽  
Kinetics Of ◽  
Amberlyst 70

A kinetic study of controlling nitrogen in process for boron steel by using30N2isotope gas

2008 ◽  
Vol 105 (12) ◽  
pp. 601-608
Author(s):  
Seung Min Han ◽  
Dong Joon Min ◽  
Joo Hyun Park ◽  
Jung Ho Park ◽  
Jong Min Park
Keyword(s):  
Kinetic Study ◽  
Boron Steel

Kinetic Study of the Effect of Heparin on the Amidase Activity of Trypsin, Plasmin and Urokinase

1983 ◽  
Vol 49 (03) ◽  
pp. 199-203 ◽  
Author(s):  
V M Yomtova ◽  
N A Stambolieva ◽  
B M Blagoev
Keyword(s):  
Kinetic Study ◽  
Active Center ◽  
Simultaneous Presence ◽  
Amidase Activity ◽  
Competitive Inhibitors ◽  
Uncompetitive Inhibitor

SummaryIt was found that the effect of heparin on the amidase activity of urokinase (E C 3.4.21.31), plasmin (E C 3.4.21.7) and trypsin (E C 3.4.21.4) depended on the substrate used. No effect of heparin on the amidase activity of urokinase and trypsin was observed when Pyro Glu-Gly-Arg-p-nitroanilide (S-2444) and α-N-acetyl-L-lysine-p-nitroanilide (ALNA) were used as substrates. Heparin acted as a uncompetitive inhibitor of trypsin (Ki = 1.2×10-6 M), plasmin (Ki = 4.9×10-6 M) and urokinase (Ki = l.0×10-7 M) when Bz-Phe-Val-Arg-p-nitroanilide (S-2160), H-D-Val-Leu-Lys-p-nitroanilide (S-2251) and plasminogen, respectively, were used as substrates. These results, as well as the data obtained by studying the effect of the simultaneous presence of heparin and competitive inhibitors suggest that although heparin is not bound at the active center of these enzymes, it may influence the effectivity of catalysis.

A kinetic study of the metathesis of propene on a rhenium-aluminium catalyst

1981 ◽  
Vol 31 (1) ◽  
pp. 388-394 ◽  
Author(s):  
Mahmoud El-Sawi ◽  
Antonio Iannibello ◽  
Fernando Morelli ◽  
Ganfranco Gatalano ◽  
Francesco Intrieri ◽  
...  
Keyword(s):  
Kinetic Study
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