Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Anton Wangler"'
Publikováno v:
ACS Omega, Vol 4, Iss 4, Pp 6264-6272 (2019)
Externí odkaz:
https://doaj.org/article/8a8102bc364e4845a0a1d9f3ecdcf05c
Publikováno v:
ACS Omega, Vol 3, Iss 2, Pp 1783-1790 (2018)
Externí odkaz:
https://doaj.org/article/613b55b859cf40d89bdff05e1223bf90
Publikováno v:
Trends in Biotechnology. 37:1038-1041
To improve the kinetics of enzyme-catalyzed reactions, cosolvents are commonly added to reaction mixtures. The search for a good cosolvent is still empirical and experimentally based. We discuss a thermodynamic activity-based approach that improves b
Publikováno v:
The Journal of Chemical Thermodynamics. 128:275-282
The use of co-solvents for the enhancement of the reaction parameters reaction rate, yield and enantioselectivity is an established optimization strategy in biotechnology. To determine the influence of co-solvents on even one of these reaction parame
Autor:
Gabriele Sadowski, Michael Knierbein, Christoph Held, Anton Wangler, Roland Winter, Trung Quan Luong
Publikováno v:
Physical Chemistry Chemical Physics. 21:22224-22229
The application of co-solvents and high pressure has been reported to be an efficient means to tune the kinetics of enzyme-catalyzed reactions. Co-solvents and pressure can lead to increased reaction rates without sacrificing enzyme stability, while
Publikováno v:
Fluid Phase Equilibria. 461:15-27
The major goal of this work was the prediction of the solubility of CO 2 and H 2 S in aqueous methyldiethanolamine ( MDEA ) reacting systems using the electrolyte equation of state ePC-SAFT with focus on MDEA weight fractions wMDEA> 0.3 (related to t
Autor:
Sergey P. Verevkin, Anton Wangler, Trung Quan Luong, Roberto I. Canales, Roland Winter, Christoph Held, Gabriele Sadowski, Dzmitry H. Zaitsau
Publikováno v:
Physical Chemistry Chemical Physics. 20:11317-11326
This work presents an approach that expresses the Michaelis constant KaM and the equilibrium constant Kth of an enzymatic peptide hydrolysis based on thermodynamic activities instead of concentrations. This provides KaM and Kth values that are indepe
Publikováno v:
Chemistry (Weinheim an der Bergstrasse, Germany). 24(61)
Co-solvents are known to influence the Michaelis constant K M of enzyme-catalyzed reactions. In the literature, co-solvent effects on K M are usually explained by interactions between enzyme and co-solvent. Very recent works replaced substrate concen