Lipase TL®-mediated kinetic resolution of benzoin: facile synthesis of (1R,2S)-erythro-2-amino-1,2-diphenylethanol

Aoyagi, Yutaka; Agata, Naoki; Shibata, Noriko; Horiguchi, Mai; Williams, Robert M.

doi:10.1016/s0040-4039(00)01832-3

Cited by 37 publications

(14 citation statements)

References 11 publications

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“…co.jp/meito/kaseihin/index e.html) has proven to be an attractive alternative for the recognition of alcohols possessing large groups at the asymmetric carbon atom, such as wood sterols [10], benzoins [11][12][13] and other bulky secondary alcohols [14][15][16]. On the other hand, this enzyme has been shown to be very active in hydrophobic solvents, such as toluene [15], or polar ones, such as acetone, 1,4-dioxane [16] or THF [11][12][13][14], also displaying an increase in activity and stability upon immobilization [17]. Furthermore, Lipase TL has proven to be also useful for N-acetylalanine deprotection [18], stereoselective acylation of 2-chloro-1-(2,4-difluorophenyl)ethanol [19] or aminolysis reactions [20] in 2-methyltetrahydrofuran (2-MeTHF), a greener substitute for THF displaying very interesting properties.…”

Section: Introductionmentioning

confidence: 99%

Lipase from Pseudomonas stutzeri: Purification, homology modelling and rational explanation of the substrate binding mode

Maraite

Hoyos²,

Carballeira³

et al. 2013

Journal of Molecular Catalysis B: Enzymatic

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Section: Introductionmentioning

confidence: 99%

Lipase from Pseudomonas stutzeri: Purification, homology modelling and rational explanation of the substrate binding mode

Maraite

Hoyos²,

Carballeira³

et al. 2013

Journal of Molecular Catalysis B: Enzymatic

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“…Success was evaluated with regard to the specic catalytic activity of the resulting immobilisates in the trans-esterication of benzoin with vinyl butyrate using tetrahydrofuran (THF) as solvent. 4,10 The immobilised preparation is further denoted as Acc-LipTL.…”

Section: Immobilisation Of Lipase Tl®mentioning

confidence: 99%

Combined heterogeneous bio- and chemo-catalysis for dynamic kinetic resolution of (rac)-benzoin

et al. 2014

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Dynamic kinetic resolution (DKR) of racemic starting material is a promising route to optically pure (S)-benzoin (2-hydroxy-1,2-di(phenyl)ethanone) and various symmetrical and unsymmetrical derivatives thereof. Here, this route was advanced towards technical scale synthesis using the basic (rac)-benzoin as model system. The reaction employed stereoselective transesterification of (S)-benzoin with lipase TL® from Pseudomonas stutzeri and racemization of (R)-benzoin with Metal-TUD-1, a metal-associated acidic meso-porous silicate, in pure organic solvent. Enzyme performance was improved by immobilization on Accurel MP1001 (yielding Acc-LipTL), and Zr-TUD-1 (Si/Zr = 25) was identified as most effective racemization catalyst. Compatibility in solvent and temperature dependency enabled performance in only one pot. DKR in toluene at 50 °C yielded conversions above 98% and an ee of >97% in only five hours. Stability of Acc-LipTL was further improved with polyethylene imine and the reaction system was then reused in five cycles, retaining a conversion of >99% and a product-ee of >98%. On a semi-preparative scale, the isolated yield of enantiopure (S)-benzoin butyrate was >98%. Thus, the system provides a good basis for synthesis of enantiopure benzoin, and potentially a broader range of aromatic α-hydroxy ketones

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“…Further enzymological analysis of this enzyme is in progress and will elucidate substrate speci®city and a mechanism of the asymmetric reduction. Benzoin is utilized as a source to synthesize chiral stationary phase for HPLC, chiral auxiliaries in symmetric synthesis, and analytical reagents (Aoyagi et al, 2000;Davis et al, 1989;Oong, 1994). Therefore, investigation of the B. cereus benzil reductase may be useful to produce optically pure compounds including benzoin from diketone compounds.…”

Section: Overexpression Of B Cereus Benzil Reductase In E Colimentioning

confidence: 99%

Isolation and expression of a Bacillus cereus gene encoding benzil reductase

Maruyama

Nishizawa

Itoi³

et al. 2001

Biotech & Bioengineering

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Benzil was reduced stereospecifically to (S)-benzoin by Bacillus cereus strain Tim-r01. To isolate the gene responsible for asymmetric reduction, we constructed a library consisting of Escherichia coli clones that harbored plasmids expressing Bacillus cereus genes. The library was screened using the halo formation assay, and one clone showed benzil reduction to (S)-benzoin. Thus, this clone seemed to carry a plasmid encoding a Bacillus cereus benzil reductase. The deduced amino acid sequence had marked homologies to the Bacillus subtilis yueD protein (41% identity), the yeast open reading frame YIR036C protein (31%), and the mammalian sepiapterin reductases (28% to 30%), suggesting that benzil reductase is a novel short-chain de-hydrogenases/ reductase.

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Lipase TL®-mediated kinetic resolution of benzoin: facile synthesis of (1R,2S)-erythro-2-amino-1,2-diphenylethanol

Cited by 37 publications

References 11 publications

Lipase from Pseudomonas stutzeri: Purification, homology modelling and rational explanation of the substrate binding mode

Lipase from Pseudomonas stutzeri: Purification, homology modelling and rational explanation of the substrate binding mode

Combined heterogeneous bio- and chemo-catalysis for dynamic kinetic resolution of (rac)-benzoin

Isolation and expression of a Bacillus cereus gene encoding benzil reductase

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