Kinetic study on enantioselective resolution of ( R,S )‐2‐phenylpropionic acid through Novozyme 435–catalyzed esterification

2019 ◽  
Vol 51 (7) ◽  
pp. 520-527 ◽  
Author(s):  
Xin Yuan ◽  
Panliang Zhang ◽  
Weifeng Xu ◽  
Kewen Tang
Keyword(s):  
Kinetic Study ◽  
Phenylpropionic Acid ◽  
Novozyme 435 ◽  
Enantioselective Resolution

scholarly journals Towards sustainable kinetic resolution, a combination of bio-catalysis, flow chemistry and bio-based solvents

2018 ◽  
Vol 20 (1) ◽  
pp. 136-140 ◽  
Author(s):  
Andree Iemhoff ◽  
James Sherwood ◽  
Con R. McElroy ◽  
Andrew J. Hunt
Keyword(s):  
Kinetic Resolution ◽  
Flow Chemistry ◽  
Model System ◽  
Phenylpropionic Acid ◽  
Novozyme 435

The esterification of 2-phenylpropionic acid was investigated as a model system for enzyme catalysed (CALB, Novozyme 435) reactions in bio-based solvents.

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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