ISSN:
1432-0614
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
Abstract A purified and partially characterized novel NADP+–dependent oxidoreductase from Clostridium tyrobutyricum DSM 1460 was applied for the preparative reduction of several 3-oxo acids to (S)–3-hydroxy acids. (R)-3-Hydroxybutyrate was prepared by the same enzyme selectively dehydrogenating the S enantiomer of (R,S)-3-hydroxybutyrate. The enantiomeric purity of the (S)- and (R)-3-hydroxy acids was at least 98% enantiomeric excess (e.e.). NADPH for reductions and NADP+ for dehydrogenations were regenerated by applying artificial mediator accepting pyridine nucleotide oxidoreductases in the form of a crude extract of C. thermoaceticum cells. For NADP+ regeneration also the system 2-oxoglutarate/glutamate dehydrogenase was used for comparison. Instead of the purified (S)-3-hydroxycarboxylate oxidoreductase, resting cells of C. tyrobutyricum were also applied for reductions and dehydrogenations with substrate concentrations of 200–400 mM leading to products with e.e. values above 96%.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/s002530050291
