Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Rüdiger Ohs"'
Publikováno v:
Biotechnology Progress. 34:1081-1092
Thiamine diphosphate (ThDP)-dependent enzymes catalyze a broad range of reactions with excellent enantioselectivity. Among these reactions, carboligations of aldehydes are of particular interest since the products, chiral hydroxy ketones, are valuabl
Publikováno v:
IFAC-PapersOnLine. 51:753-758
The dynamic models used for biological and chemical process analysis and design usually include a significant number of uncertain model parameters. Sensitivity analysis is frequently applied to provide quantitative information regarding the influence
Publikováno v:
AIChE Journal. 63:4870-4880
Progress curve experiments combined with optimal experimental design (OED) are an efficient approach to determine enzyme kinetics. However, it is hardly possible to verify why specific experiments are suggested for nonlinear enzyme kinetic model iden
Publikováno v:
Biotechnology Progress. 35
The kinetic description of enzyme-catalyzed reactions is a core task in biotechnology and biochemical engineering. In particular, mechanistic kinetic models help from the discovery of the biocatalyst throughout its application. Chemo- or enantioselec
Autor:
Werner Eberhard, Anita B. Ogolong, Antje C. Spiess, Jens Begemann, Marion B. Ansorge-Schumacher, Rüdiger Ohs
Publikováno v:
Process Biochemistry. 51:1397-1405
A novel control concept was developed for a two phase biocatalytic oxidoreduction system. The hydrophobic substrate acetophenone dissolved in n -heptane is reduced to ( S )-1-phenylethanol by Candida parapsilosis carbonyl reductase 2, immobilized in
Publikováno v:
Biotechnology Journal. 14:1800183
The estimation of kinetic parameters provides valuable insights into the function of biocatalysts and is indispensable in optimizing process conditions. Frequently, kinetic analysis relies on the Michaelis-Menten model derived from initial reaction r