Purification and Characterization of a Yeast Carbonyl Reductase for Synthesis of Optically Active (<i>R</i>)-Styrene Oxide Derivatives

Kizaki, Noriyuki; Sawa, Ikuo; Yano, Miho; Yasohara, Yoshihiko; Hasegawa, Junzo

doi:10.1271/bbb.69.79

Cited by 20 publications

(10 citation statements)

References 26 publications

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“…[20], and Rhodococcus sp. [21], along with yeasts including Rhodotorula glutinis [22], Candida parapsilosis [23], and Geotrichum candidum [24]. From the comparison provided in Table 3, it can be seen that, among specific bacterial ADHs whose activity on 2-butanone has been characterized, LbADH shows among the highest affinities.…”

Section: Comparing Lbadh With Other Bacterial Adhsmentioning

confidence: 99%

Activity of Lactobacillus brevis Alcohol Dehydrogenase on Primary and Secondary Alcohol Biofuel Precursors

et al. 2015

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The R-specific alcohol dehydrogenase (ADH) from Lactobacillus brevis LB19 (LbADH) was studied with respect to its ability to reduce a series of 3-through 5-carbon 2-alkanones and aldehydes of relevance as biofuel precursors. Although active on all substrates tested, LbADH displays a marked preference for longer chain substrates. Interestingly, however, 2-alkanones were found to impose substrate inhibition towards LbADH, whereas aldehyde substrates rendered no such effect. Inhibition caused by 2-alkanones was furthermore found to intensify with increasing chain length. Despite demonstrating both primary and secondary ADH activities, a preliminary sequence analysis suggests that LbADH remains distinct from other, previously characterized primary-secondary ADHs. In addition to further characterizing the substrate range of this industrially important enzyme, this study suggests that LbADH has the potential to serve as a useful enzyme for the engineering of various novel alcohol biofuel pathways.

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Section: Comparing Lbadh With Other Bacterial Adhsmentioning

confidence: 99%

Activity of Lactobacillus brevis Alcohol Dehydrogenase on Primary and Secondary Alcohol Biofuel Precursors

et al. 2015

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“…Both ( S )-(+)- as well as ( R )-(−)-2-bromo-1-(4'-chlorophenyl)-ethan-1-ol ( 2c ) can be obtained by chemical methods [ 36 , 39 ]. In literature there are twenty microbial strains described that can reduce 2-bromo-4'-chloroacetophenone ( 1c ) to compound 2c [ 38 , 40 ]. Among them, the highest substrate conversion (89%) was noted in the culture of Candida magnoliae IFO11, however, the enantiomeric excess of the alcohol obtained was only 68%.…”

Section: Resultsmentioning

confidence: 99%

Highly Enantioselective Production of (R)-Halohydrins with Whole Cells of Rhodotorula rubra KCh 82 Culture

Janeczko

Dymarska

Kostrzewa-Susłow

2014

IJMS

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Biotransformation of ten α-haloacetophenones in the growing culture of the strain Rhodotorula rubra KCh 82 has been carried out. Nine of the substrates underwent an effective enantioselective reduction to the respective (R)-alcohols according to Prelog’s rule, with the exception of 2-chloro-1,2-diphenylethan-1-one that was not transformed by this strain. The expected reduction proceeded without dehalogenation, leading to the respective (R)-halohydrins in high yields. The use of this biocatalyst yielded (R)-2-bromo-1-phenyl-ethan-1-ol (enantiomeric excess (ee) = 97%) and its derivatives: 4'-Bromo- (ee = 99%); 4'-Chloro- (ee > 99%); 4'-Methoxy- (ee = 96%); 3'-Methoxy- (ee = 93%); 2'-Methoxy- (ee = 98%). There were also obtained and characterized 2,4'-dichloro-, 2,2',4'-trichloro- and 2-chloro-4'-fluoro-phenyetan-1-ol with >99% of enantiomeric excesses.

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“…A recombinant carbonyl reductase from Candida magnoliae co‐expressed with a GDH catalyzed the reduction of 200 g/L ( S )‐CHOH to prepare (3 R ,5 S )‐CDHH with 97.2% yield and 98.6% d.e . with 303.8 g/L glucose for NADP + regeration . Gong et al harbored engineered E. coli strain containing carbonyl reductase from Lactobacillus brevis and GDH to catalyze the biosynthesis of tert ‐butyl‐6‐cyano‐(3 R ,5 R )‐dihydroxyhexanoate with >99.5% d.e .…”

Section: Discussionmentioning

confidence: 99%

“…Kizaki et al employed a highly efficient CR from Canadian magnoliae IFO 0705, co‐expressed with a GDH form Exiguobacterium sibiricum , to transform 200 g/L ( S )‐CHOH to (3 R ,5 S )‐CDHH, resulting in a yield of 97.2% and e.e . of 98.6% . In our recent study, a mutant carbonyl reductase Rt SCR9‐mut‐Ile144Lys ( R 9M) was obtained from Rhodosporidium toruloides showing a capability to catalyze 1 M (237 g) ( S )‐CHOH to (3 R ,5 S )‐CDHH with a yield of >98.0% and e.e .…”

Section: Introductionmentioning

confidence: 99%

Production of tert‐butyl (3R,5S)‐6‐chloro‐3,5‐dihydroxyhexanoate using carbonyl reductase coupled with glucose dehydrogenase with high space–time yield

Zhang

Zheng

et al. 2019

Biotechnology Progress

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tert-Butyl (3R,5S)-6-chloro-3,5-dihydroxyhexanoate ((3R,5S)-CDHH) is an important chiral intermediate for the synthesis of rosuvastatin. The biotechnological production of (3R,5S)-CDHH is catalyzed from tert-butyl (S)-6-chloro-5-hydroxy-3-oxohexanoate ((S)-CHOH) by a carbonyl reductase, and this synthetic pathway is becoming a primary route for (3R,5S)-CDHH production due to its high enantioselectivity, mild reaction conditions, low cost, process safety, and environmental friendship. However, the requirement of the pyridine nucleotide cofactors, reduced nicotinamide adenine dinucleotide (NADH) or reduced nicotinamide adenine dinucleotide phosphate (NADPH) limits its economic flexibility. In the present study, a recombinant Escherichia coli strain harboring carbonyl reductase R9M and glucose dehydrogenase (GDH) was constructed with high carbonyl reduction activity and cofactor regeneration efficiency. The recombinant E. coli cells were applied for the efficient production of (3R,5S)-CDHH with a substrate conversion of 98.8%, a yield of 95.6% and an enantiomeric excess (e.e.) of >99.0% under 350 g/L of (S)-CHOH after 12 hr reaction. A substrate fed-batch strategy was further employed to increase the substrate concentration to 400 g/L resulting in an enhanced product yield to 98.5% after 12 hr reaction in a 1 L bioreactor. Meanwhile, the space-time yield was 1,182.3 g L −1 day −1 , which was the highest value ever reported by a coupled system of carbonyl reductase and glucose dehydrogenase. K E Y W O R D Scarbonyl reductase, co-expression, glucose dehydrogenase, tert-butyl (3R,5S)-6-chloro-3,5-dihydroxyhexanoate

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Purification and Characterization of a Yeast Carbonyl Reductase for Synthesis of Optically Active (R)-Styrene Oxide Derivatives

Cited by 20 publications

References 26 publications

Activity of Lactobacillus brevis Alcohol Dehydrogenase on Primary and Secondary Alcohol Biofuel Precursors

Activity of Lactobacillus brevis Alcohol Dehydrogenase on Primary and Secondary Alcohol Biofuel Precursors

Highly Enantioselective Production of (R)-Halohydrins with Whole Cells of Rhodotorula rubra KCh 82 Culture

Production of tert‐butyl (3R,5S)‐6‐chloro‐3,5‐dihydroxyhexanoate using carbonyl reductase coupled with glucose dehydrogenase with high space–time yield

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