Reduction of Ketones and Aldehydes to Alcohols

Gröger, Harald; Hummel, Werner; Borchert, Sonja; Kraußer, Marina

doi:10.1002/9783527639861.ch26

Cited by 11 publications

(9 citation statements)

References 270 publications

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“…Asymmetric reduction of ketones by non-biological (Yoshimura et al 2014;Shende et al 2018) and biological catalysts (Matsuda et al 2009;Ni and Xu 2012;Gröger et al 2012;Rosenthal and Lütz 2018) is one of the most straightforward ways to access enantiomerically pure alcohols beneficial for pharmaceutical and agrochemical intermediates. In particular, biological catalysts or enzymes are considered a sustainable catalyst for pharmaceutical intermediates.…”

Section: Introductionmentioning

confidence: 99%

Structural basis for a highly (S)-enantioselective reductase towards aliphatic ketones with only one carbon difference between side chain

Koesoema

Sugiyama

et al. 2019

Appl Microbiol Biotechnol

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Aliphatic ketones, such as 2-butanone and 3-hexanone, with only one carbon difference among side chains adjacent to the carbonyl carbon are difficult to be reduced enantioselectively. In this study, we utilized an acetophenone reductase from Geotrichum candidum NBRC 4597 (GcAPRD) to reduce challenging aliphatic ketones such as 2-butanone (methyl ethyl ketone) and 3-hexanone (ethyl propyl ketone) to their corresponding (S)-alcohols with 94% ee and > 99% ee, respectively. Through crystallographic structure determination, it was suggested that residue Trp288 limit the size of the small binding pocket. Docking simulations imply that Trp288 plays an important role to form a C-H⋯π interaction for proper orientation of ketones in the pro-S binding pose in order to produce (S)-alcohols. The excellent (S)-enantioselectivity is due to a non-productive pro-R binding pose, consistent with the observation that the (R)-alcohol acts as an inhibitor of (S)-alcohol oxidation.

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Section: Introductionmentioning

confidence: 99%

Structural basis for a highly (S)-enantioselective reductase towards aliphatic ketones with only one carbon difference between side chain

Koesoema

Sugiyama

et al. 2019

Appl Microbiol Biotechnol

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“…Not only bulky–nonbulky substrates with major size differences between the two substituents, but also bulky–bulky substrates such as diaryl ketones can be reduced to enantiopure alcohols. 80,88–92 …”

Section: Stereoselective Reactions Involving Transformations Of Sp 2 Carbonsmentioning

confidence: 99%

Enzymatic strategies for asymmetric synthesis

Hall

2021

RSC Chem. Biol.

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“…Additionally, whole cells are able to perform multi-step microbial bioconversions and co-factor recycling [ 31 , 32 ]. The conversion of benzaldehyde to benzyl alcohol in microbial cells may be catalyzed by aldehyde dehydrogenases (ALDHs), alcohol dehydrogenases (ADHs), and/or aldo-keto reductases, which are enzymes able to catalyze the reversible reduction of aldehydes, ketones, and/or keto esters to the corresponding alcohol with consumption of NADH or NADPH [ 33 , 34 , 35 ].…”

Section: Introductionmentioning

confidence: 99%

Process Development for Benzyl Alcohol Production by Whole-Cell Biocatalysis in Stirred and Packed Bed Reactors

Rodrigues

Carvalho

2022

Microorganisms

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The ocean is an excellent source for new biocatalysts due to the tremendous genetic diversity of marine microorganisms, and it may contribute to the development of sustainable industrial processes. A marine bacterium was isolated and selected for the conversion of benzaldehyde to benzyl alcohol, which is an important chemical employed as a precursor for producing esters for cosmetics and other industries. Enzymatic production routes are of interest for sustainable processes. To overcome benzaldehyde low water solubility, DMSO was used as a biocompatible cosolvent up to a concentration of 10% (v/v). A two-phase system with n-hexane, n-heptane, or n-hexadecane as organic phase allowed at least a 44% higher relative conversion of benzaldehyde than the aqueous system, and allowed higher initial substrate concentrations. Cell performance decreased with increasing product concentration but immobilization of cells in alginate improved four-fold the robustness of the biocatalyst: free and immobilized cells were inhibited at concentrations of benzyl alcohol of 5 and 20 mM, respectively. Scaling up to a 100 mL stirred reactor, using a fed-batch approach, enabled a 1.5-fold increase in benzyl alcohol productivity when compared with batch mode. However, product accumulation in the reactor hindered the conversion. The use of a continuous flow reactor packed with immobilized cells enabled a 9.5-fold increase in productivity when compared with the fed-batch stirred reactor system.

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Reduction of Ketones and Aldehydes to Alcohols

Cited by 11 publications

References 270 publications

Structural basis for a highly (S)-enantioselective reductase towards aliphatic ketones with only one carbon difference between side chain

Structural basis for a highly (S)-enantioselective reductase towards aliphatic ketones with only one carbon difference between side chain

Enzymatic strategies for asymmetric synthesis

Process Development for Benzyl Alcohol Production by Whole-Cell Biocatalysis in Stirred and Packed Bed Reactors

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