Abstract:
:Enzyme-catalyzed asymmetric reduction of ethyl 4-chloro-3-oxobutanoate in an organic solvent-water diphasic system was studied. NADPH-dependent aldehyde reductase isolated from Sporobolomyces salmonicolor AKU4429 and glucose dehydrogenase were used as catalysts for reduction of ethyl 4-chloro-3-oxobutanoate and recycling of NADPH, respectively, in this system. In an aqueous system, the substrate was unstable. Inhibition of the reaction and inactivation of the enzymes by the substrate and the product were also observed. An n-butyl acetate-water diphasic system very efficiently overcame these limitations. In a 1,600-ml-1,600-ml scale diphasic reaction, ethyl (R)-4-chloro-3-hydroxybutanoate (0.80 mol; 86% enantiomeric excess) was produced from the corresponding oxoester in a molar yield of 95.4% with an NADPH turnover of 5,500 mol/mol.
journal_name
Appl Environ Microbioljournal_title
Applied and environmental microbiologyauthors
Shimizu S,Kataoka M,Katoh M,Morikawa T,Miyoshi T,Yamada Hdoi
10.1128/AEM.56.8.2374-2377.1990keywords:
subject
Has Abstractpub_date
1990-08-01 00:00:00pages
2374-2377issue
8eissn
0099-2240issn
1098-5336journal_volume
56pub_type
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