‘Low-temperature method’ for a dramatic improvement in enantioselectivity in lipase-catalyzed reactions

Sakai, Takashi

doi:10.1016/j.tetasy.2004.07.058

Cited by 102 publications

(22 citation statements)

References 58 publications

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“…However, further increase in temperature led to a sharp drop in the yield, which could be attributed to the partial inactivation of the cells at higher temperature. On the contrary, the product ee decreased gradually with the increase in temperature, which was consistent with the generally reported results that lower temperature favored the enhancement of the enantioselectivity [30]. Taking into account the yield and ee of the product, the optimum temperature was established to be 25°C, when the yield and ee were 73.9 and 95.4%, respectively.…”

Section: Effect Of Temperature On the Bioreductionsupporting

confidence: 89%

Integration of newly isolated biocatalyst and resin-based in situ product removal technique for the asymmetric synthesis of (R)-methyl mandelate

Guo

2009

Bioprocess Biosyst Eng

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The enantioselective reduction of methyl benzoylformate to (R)-methyl mandelate, an important pharmaceutical intermediate and a versatile resolving agent, was investigated in this study. After minimizing the reaction-specific constraints (constraints dependent on the nature of the substrate and product) by preliminary selection of the reaction parameters, an effective whole cell biocatalyst (Saccharomyces cerevisiae AS2.1392) was obtained by simple screening procedures. Under further optimized conditions, a product concentration of 103 mmol L(-1) could be attained within 5 h with a yield of 85.8% and an enantiometric excess of 95.4%, indicating S. cerevisiae AS2.1392 an efficient biocatalyst for the asymmetric synthesis of (R)-methyl mandelate. Furthermore, resin-based in situ product removal (ISPR) technique was applied to alleviate the substrate and product inhibition or toxicity to the whole cells. The integration of newly isolated biocatalyst and proper ISPR technique provides a practical route for the preparation of optically active pharmaceutical intermediates.

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Section: Effect Of Temperature On the Bioreductionsupporting

confidence: 89%

Integration of newly isolated biocatalyst and resin-based in situ product removal technique for the asymmetric synthesis of (R)-methyl mandelate

Guo

2009

Bioprocess Biosyst Eng

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“…Similar phenomena of the decrease in e.e. p derived from reaction temperature increase were also observed in protease (Miyazawa et al 1997) and lipase (López-Serrano et al 2001;Sakai 2004;Sakai et al 1998) catalyzed biotransformations. Our findings were consistent with the widely believed view that temperature plays an important role in activity and enantioselectivity of biocatalysts (Phillips 1996).…”

Section: Effect Of Phmentioning

confidence: 84%

Characterization of an enantioselective amidase with potential application to asymmetric hydrolysis of (R, S)-2, 2-dimethylcyclopropane carboxamide

Wang

Cheng

Zheng

et al. 2011

World J Microbiol Biotechnol

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Amidase is a promising synthesis tool for chiral amides and related derivatives. In the present study, the biochemical properties of the Delftia tsuruhatensis CCTCC M 205114 enantioselective amidase were determined for its potential application in chiral amides synthesis. D. tsuruhatensis CCTCC M 205114 amidase was purified 105.2 fold with total activity recovery of 4.26%. The enzyme is a monomer with a subunit of approximately 50 kDa by analytical gel filtration HPLC and SDS-PAGE. It had a broad substrate spectrum and displayed high enantioselectivity against R-2, 2-dimethylcyclopropane carboxamide and R-mandelic amide. The amidase was applied to enantioselective hydrolysis of R-2, 2-dimethylcyclopropane carboxamide from racemic (R, S)-2, 2-dimethylcyclopropane carboxamide to accumulate S-2, 2-dimethylcyclopropane carboxamide. This enzyme did not require metal ions for the hydrolysis reaction. Its optimal pH and temperature were 8.0 and 35°C, respectively. The K m and V max of the amidase for R-2, 2-dimethylcyclopropane carboxamide were 2.54 mM and 8.37 lmol min -1 mg protein -1 , respectively. After 60 min of the reaction, R-2, 2-dimethylcyclopropane carboxamide was completely hydrolyzed, generating S-2, 2-dimethylcyclopropane carboxamide with a yield of 45.9% and an e.e. of above 99%. Therefore, this amidase can serve as a promising producer for S-2, 2-dimethylcyclopropane carboxamide and other amides.

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“…In enzymecatalysed reactions, increasing temperature generally decreases selectivity. [52][53][54][55][56][57][58][59][60][61][62] In a few studies, however, enhanced selectivity with increasing temperature, 63,64 or a maximum of enantioselectivity at a certain temperature, 38,65 or even indifference to temperature was found. 66 In most of the quoted examples, the enzyme-catalysed reactions were carried out in batch mode (in stirred or shaken flasks) and only a few studies on the temperature effects on lipase-catalysed KRs were performed in continuous-flow mode so far.…”

Section: Introductionmentioning

confidence: 99%

Lipase-Catalyzed Kinetic Resolution of 1-(2-Hydroxycyclohexyl)Indoles in Batch and Continuous-Flow Systems

et al. 2014

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The lipase catalysed kinetic resolution of three trans-1-(2-hydroxycyclohexyl)-indoles in both batch and continuous-flow systems is reported. Ring opening of cyclohexene oxide by the corresponding indole followed by enzymatic acylation with vinyl acetate resulted in novel, highly enantioenriched indole-substituted cyclohexanols and cyclohexyl acetates. The effect of the temperature on enantiomeric ratio (E) and productivity (specific reaction rate, r flow ) in the continuous-flow mode acylation was studied at analytical scale in the 0-70°C range.Preparative scale kinetic resolution of the three indole derivatives was performed in mixed continuous-and recirculation-flow mode resulting in almost complete conversion and good to excellent enantiomeric purity of the products.

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‘Low-temperature method’ for a dramatic improvement in enantioselectivity in lipase-catalyzed reactions

Cited by 102 publications

References 58 publications

Integration of newly isolated biocatalyst and resin-based in situ product removal technique for the asymmetric synthesis of (R)-methyl mandelate

Integration of newly isolated biocatalyst and resin-based in situ product removal technique for the asymmetric synthesis of (R)-methyl mandelate

Characterization of an enantioselective amidase with potential application to asymmetric hydrolysis of (R, S)-2, 2-dimethylcyclopropane carboxamide

Lipase-Catalyzed Kinetic Resolution of 1-(2-Hydroxycyclohexyl)Indoles in Batch and Continuous-Flow Systems

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