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A highly stereoselective recombinant alcohol dehydrogenase aus 'Pseudomonas fluorescens' DSM50106

  • The alcohol dehydrogenase was biochemically characterized. A broad range of arylaliphatic ketones is efficiently reduced to the corresponding optically active (R)-alcohols by a recombinant alcohol dehydrogenase (PF-ADH) produced by overexpression in 'Escherichia coli'. PF-ADH shows high activity and stereoselectivity in the reduction of acetophenone and various derivatives (45-99%), as well as in the reduction of 3-oxy-butyric acid methyl ester and 3-oxy-butyric acid methyl ester and 3-oxy-hexanoic acid ethyl ester (>99%). The highest activity was observed between 10 and 20°C. The copfactor NADH can be efficiently recycled by the addition of 10-20% of iso-propanol. A flow-through-polarimetry-based assay to determine oxidoreductase activity and stereoselectivity is described.

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Author: Petra Hildebrandt
Title Additional (German):Eine hochgradig stereoselektive rekombinante Alkoholdehydrogenase aus 'Pseudomonas fluorescens' DSM50106
Advisor:Prof. Dr. Uwe Bornscheuer
Document Type:Doctoral Thesis
Date of Publication (online):2006/07/03
Granting Institution:Ernst-Moritz-Arndt-Universität, Mathematisch-Naturwissenschaftliche Fakultät (bis 31.05.2018)
Date of final exam:2005/11/26
Release Date:2006/07/03
Tag:Ketoreductase; Oxidoreductase; alcohol dehydrogenase; enantioselectivity; recombinant enzyme
GND Keyword:Oxocarbonsäureester
Faculties:Mathematisch-Naturwissenschaftliche Fakultät / Institut für Biochemie
DDC class:500 Naturwissenschaften und Mathematik / 540 Chemie