Kinetic resolution of 1-(benzofuran-2-yl)ethanols by lipase-catalyzed enantiomer selective reactions

Paizs, Csaba; Toşa, Monica Ioana; Bódai, Viktória; Szakács, George; Kmecz, Ildikó; Simándi, Béla; Majdik, Cornelia; Novák, Lajos; Irimie, Florin Dan; Poppe, László

doi:10.1016/s0957-4166(03)00358-6

Cited by 31 publications

(18 citation statements)

References 6 publications

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“…In our study, we did not use organic solvent, and on the basis of the results from key parameters optimized in a green synthesis method, we got a 92% yield of product at 42‐mmol substrate concentration with enantiopure form of ( S )‐1‐(benzofuran‐2‐yl)ethanol. The yield of benzofuran alcohol obtained with kinetic resolution in the literature is good, but this yield is low compared with asymmetric reduction . Moreover, 50% of the unwanted enantiomer always occurs at kinetic resolution.…”

Section: Resultsmentioning

confidence: 97%

“…Asymmetric bioreduction of 2‐acetylbenzo[b]furan with yeast biocatalyst gave ( S )‐corresponding alcohol with a moderate ee (55%) and in a moderate yield (60%) . Paizs and coworkers obtained ( S )‐1‐(benzofuran‐2‐yl)ethanol by 98.6% ee and 49% yield with kinetic resolution of racemic benzofuran alcohol using lipase biocatalysts . Although this yield is good for kinetic resolution, it is low for asymmetric reduction.…”

Section: Introductionmentioning

confidence: 99%

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Green synthesis of enantiopure (S)‐1‐(benzofuran‐2‐yl)ethanol by whole‐cell biocatalyst

Şahin

2019

Chirality

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Optically active aromatic alcohols are valuable chiral building blocks of many natural products and chiral drugs. Lactobacillus paracasei BD87E6, which was isolated from a cereal-based fermented beverage, was shown as a biocatalyst for the bioreduction of 1-(benzofuran-2-yl) ethanone to (S)-1-(benzofuran-2-yl) ethanol with highly stereoselectivity. The bioreduction conditions were optimized using L. paracasei BD87E6 to obtain high enantiomeric excess (ee) and conversion. After optimization of the bioreduction conditions, it was shown that the bioreduction of 1-(benzofuran-2-yl)ethanone was performed in mild reaction conditions. The asymmetric bioreduction of the 1-(benzofuran-2-yl)ethanone had reached 92% yield with ee of higher than 99.9% at 6.73 g of substrate. Our study gave the first example for enantiopure production of (S)-1-(benzofuran-2-yl)ethanol by a biological green method.This process is also scalable and has potential in application. In this study, a basic and novel whole-cell mediated biocatalytic method was performed for the enantiopure production of (S)-1-(benzofuran-2-yl)ethanol in the aqueous medium, which empowered the synthesis of a precious chiral intermediary process to be converted into a sophisticated molecule for drug production. KEYWORDS (S)-1-(benzofuran-2-yl)ethanol, asymmetric bioreduction, chirality, Lactobacillus paracasei BD87E6, whole-cell biocatalysts

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Section: Resultsmentioning

confidence: 97%

Section: Introductionmentioning

confidence: 99%

Green synthesis of enantiopure (S)‐1‐(benzofuran‐2‐yl)ethanol by whole‐cell biocatalyst

Şahin

2019

Chirality

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“…The synthesis of the investigated racemic substrates and products was rst performed using known methods [29][30][31][32][33] from the corresponding prochiral heteroaryl-methyl-ketones (1a-c,f) by chemical reduction with sodium borohydride or from the carbaldehydes (1d,e,g-i) by Grignard reaction. Racemic ethanols rac-2a-i were next transformed with acetyl chloride (1.2 equiv.)…”

Section: Chemical Synthesismentioning

confidence: 99%

“…Lipase from Pseudomonas uorescens (Amano AK), already reported as efficient, 29 demonstrated excellent selectivity for the EKR of rac-2c in neat vinyl acetate (entry 3 in Table 2); the optimal biocatalyst was obtained by sol-gel immobilization in a binary silane precursor system (AK 1 BS).…”

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confidence: 99%

Tailored sol–gel immobilized lipase preparates for the enzymatic kinetic resolution of heteroaromatic alcohols in batch and continuous flow systems

et al. 2017

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Tailored immobilized lipases from Candida antarctica B and Pseudomonas fluorescens, with improved thermal and operational stability, were prepared through fine tuning of the structure of the sol-gel matrix, using various binary or ternary precursor mixtures for the EKR of various chiral heteroaromatic secondary alcohols with benzofuran, benzo [b]thiophen, phenothiazine and 2-phenylthiazol moieties.The operational stability in batch process was studied for five selected systems by performing reuse experiments, using the conversion, enantiomeric excesses and enantiomeric ratio as parameters, demonstrating the dependence of the sol-gel lipase preparate performance on the structure of both biocatalyst and substrate. The resolution of the benzofuranic substrates with the best performing biocatalysts was studied in continuous-flow mode, using the productivity as a criterion. The specific reaction rates under continuous-flow operation (r flow ) were higher than those obtained in batch mode (r batch ) in both cases, sustaining its usefulness for further process development.

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“…Similarly, higher conversions has been reported for the synthesis of oleyl oleate [65,66], isoamyl acetate [19], isoamyl butyrate [19], ethyl palmitate [17], transesterification of benzyl alcohol, and butyl acetate [67] than in conventional solvents like acetonitrile, hexane, or toluene or under solvent-free conditions. However, there have been a few studies that indicate that some enzyme-catalyzed reactions show better yields in organic solvents compared to that obtained in supercritical fluid systems [68][69][70][71]. Alternatively, few studies show that the enzyme activities are comparable/similar in supercritical carbon dioxide and in organic solvents.…”

Section: Kinetics Of Reactionsmentioning

confidence: 99%

Effect of Chain Length on Enzymatic Hydrolysis of p-Nitrophenyl Esters in Supercritical Carbon Dioxide

Varma

Madras

2008

Appl Biochem Biotechnol

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The effect of chain length on the enzymatic hydrolysis of various p-nitrophenyl esters was investigated. Specifically, the hydrolysis of various esters p-nitrophenyl butyrate (PNPB), p-nitrophenyl caprylate (PNPC), p-nitrophenyl laurate (PNPL), p-nitrophenyl myristate (PNPM) and p-nitrophenyl palmitate (PNPP) was studied in supercritical carbon dioxide (ScCO2) with lipase (Novozym 435). This indicates that the conversion of nitrophenyl esters decreases with increasing chain length. The effect of various parameters such as amount of water added, temperature, and enzyme loading was studied. The optimum temperature for the hydrolysis of PNPB and PNPC was 50 degrees C but was 55 degrees C for PNPL, PNPM, and PNPP in ScCO2. The reactions were also conducted in acetonitrile as the solvent, and it was found that the reactions reach equilibrium much faster in ScCO2 than in acetonitrile. The kinetics of the hydrolysis reactions were modeled using a Ping Pong Bi Bi model.

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Kinetic resolution of 1-(benzofuran-2-yl)ethanols by lipase-catalyzed enantiomer selective reactions

Cited by 31 publications

References 6 publications

Green synthesis of enantiopure (S)‐1‐(benzofuran‐2‐yl)ethanol by whole‐cell biocatalyst

Green synthesis of enantiopure (S)‐1‐(benzofuran‐2‐yl)ethanol by whole‐cell biocatalyst

Tailored sol–gel immobilized lipase preparates for the enzymatic kinetic resolution of heteroaromatic alcohols in batch and continuous flow systems

Effect of Chain Length on Enzymatic Hydrolysis of p-Nitrophenyl Esters in Supercritical Carbon Dioxide

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