Asymmetric reduction of ketones by the acetone powder of Geotrichum candidum

Nakamura, Kaoru; Kitano, Kazutada; Matsuda, Tomoko; Ohno, Atsuyoshi

doi:10.1016/0040-4039(96)00073-1

Cited by 67 publications

(41 citation statements)

References 13 publications

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“…However, except for very few examples (Baratta et al, 2008;Evans et al, 2003;Zeror et al, 2008), use of these catalysts was prohibited by insufficient enantioselectiviy. Several microbial and plant cells inheriting o-chloroacetophenone reductase activity have been identified by extensive screening recently (Andrade et al, 2005(Andrade et al, , 2009Kagohara et al, 2008;Kurbanoglu et al, 2007aKurbanoglu et al, ,b, 2010Nakamura and Matsuda, 1998;Ou et al, 2008;Salvi and Chattopadhyay, 2008;Xie et al, 2006). However, the number of isolated and characterized enzymes (Gröger et al, 2006;Itoh et al, 1999;Yang et al, 2007;Zhu et al, 2006) exhibiting o-chloroacetophenone reductase activity is still limited.…”

Section: Introductionmentioning

confidence: 96%

Enzyme identification and development of a whole‐cell biotransformation for asymmetric reduction ofo‐chloroacetophenone

Kratzer

Pukl

Egger

et al. 2010

Biotech & Bioengineering

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Chiral 1-(o-chlorophenyl)-ethanols are key intermediates in the synthesis of chemotherapeutic substances. Enantioselective reduction of o-chloroacetophenone is a preferred method of production but well investigated chemo- and biocatalysts for this transformation are currently lacking. Based on the discovery that Candida tenuis xylose reductase converts o-chloroacetophenone with useful specificity (kcat/Km=340 M(-1) s(-1)) and perfect S-stereoselectivity, we developed whole-cell catalysts from Escherichia coli and Saccharomyces cerevisiae co-expressing recombinant reductase and a suitable system for recycling of NADH. E. coli surpassed S. cerevisiae sixfold concerning catalytic productivity (3 mmol/g dry cells/h) and total turnover number (1.5 mmol substrate/g dry cells). o-Chloroacetophenone was unexpectedly "toxic," and catalyst half-life times of only 20 min (E. coli) and 30 min (S. cerevisiae) in the presence of 100 mM substrate restricted the time of batch processing to maximally ∼5 h. Systematic reaction optimization was used to enhance the product yield (≤60%) of E. coli catalyzed conversion of 100 mM o-chloroacetophenone which was clearly limited by catalyst instability. Supplementation of external NAD+ (0.5 mM) to cells permeabilized with polymyxin B sulfate (0.14 mM) resulted in complete conversion providing 98 mM S-1-(o-chlorophenyl)-ethanol. The strategies considered for optimization of reduction rate should be generally useful, however, especially under process conditions that promote fast loss of catalyst activity.

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Section: Introductionmentioning

confidence: 96%

Enzyme identification and development of a whole‐cell biotransformation for asymmetric reduction ofo‐chloroacetophenone

Kratzer

Pukl

Egger

et al. 2010

Biotech & Bioengineering

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“…6 Using resting cells of Candida tropicalis, 3 -fluoroacetophenone (1) could be reduced with 97% ee ((S)-enantiomer). 7 Moreover, the literature 8 indicated that the most efficient reduction methods were enzymatic with >99% ee, however, the reactions catalyzed by enzymes demand cofactors, which are often too expensive.…”

Section: Introductionmentioning

confidence: 99%

Production of (R)‐3′‐fluorophenylethan‐1‐ol by Trichothecium roseum isolate in a laboratory scale bioreactor

Kurbanoğlu

Taşkın

Zilbeyaz

et al. 2009

J of Chemical Tech & Biotech

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BACKGROUND: Enantiomerically pure, fluorinated compounds play an important role in medicinal chemistry. Trichothecium roseum strains were isolated for the production of (R)-3 -fluorophenylethan-1-ol. Biocatalytic production of optically active (R)-3 -fluorophenylethan-1-ol was achieved by asymmetric reduction of 3 -fluoroacetophenone in a batch culture of Trichothecium roseum using ram horn peptone (RHP). The reaction conditions (pH, temperature and agitation) required to improve the conversion of 3 -fluoroacetophenone and enantiomeric excess (ee) of (R)-3 -fluorophenylethan-1-ol were studied.

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“…Chemicals 2¢,4¢-Dichloroacetophenone (Table 1, 1), m-chlorophenacyl chloride (2), 3¢-methoxyacetophenone (3), 3,4-dimethoxyphenylacetone (4), N-Boc-3-pyrrolidinone (5), methyl 4-bromo-3-oxobutanoate (14), ethyl 4-bromo-3-oxobutanoate (15), isopropyl 4-bromo-3-oxobutanoate (16), octyl 4-bromo-3-oxobutanoate (17), isopropyl 4-cyano-3-oxobutanoate (18)…”

Section: A T E R I a L S A N D M E T H O D Smentioning

confidence: 99%

“…Acetone powder of the fungus Geotrichum candidum cells gave (S)-alcohols from acetophenone derivatives with an optical purity of 99% e.e. [4,5]. However, such a microbial process is not yet of practical use because of the low product accumulation.…”

mentioning

confidence: 99%

Chiral alcohol production by NADH‐dependent phenylacetaldehyde reductase coupled with in situ regeneration of NADH

Itoh

Matsuda

Mabuchi

et al. 2002

European Journal of Biochemistry

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Phenylacetaldehyde reductase (PAR) produced by styreneassimilating Corynebacterium strain ST-10 was used to synthesize chiral alcohols. This enzyme with a broad substrate range reduced various prochiral aromatic ketones and b-ketoesters to yield optically active secondary alcohols with an enantiomeric purity of more than 98% enantiomeric excess (e.e.). The Escherichia coli recombinant cells which expressed the par gene could efficiently produce important pharmaceutical intermediates; (R)-2-chloro-1-(3-chlorophenyl)ethanol (28 mgAEmL )1 ) from m-chlorophenacyl chloride, ethyl (R)-4-chloro-3-hydroxy butanoate) (28 mgAEmL )1 ) from ethyl 4-chloro-3-oxobutanoate and (S)-N-tert-butoxycarbonyl(Boc)-3-pyrrolidinol from N-Boc-3-pyrrolidinone (51 mgAEmL )1 ), with more than 86% yields. The high yields were due to the fact that PAR could concomitantly reproduce NADH in the presence of 3-7% (v/v) 2-propanol in the reaction mixture. This biocatalytic process provided one of the best asymmetric reductions ever reported.

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Asymmetric reduction of ketones by the acetone powder of Geotrichum candidum

Cited by 67 publications

References 13 publications

Enzyme identification and development of a whole‐cell biotransformation for asymmetric reduction ofo‐chloroacetophenone

Enzyme identification and development of a whole‐cell biotransformation for asymmetric reduction ofo‐chloroacetophenone

Production of (R)‐3′‐fluorophenylethan‐1‐ol by Trichothecium roseum isolate in a laboratory scale bioreactor

Chiral alcohol production by NADH‐dependent phenylacetaldehyde reductase coupled with in situ regeneration of NADH

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