Engineering Aspects of Enzyme

Kragl, Udo; Niedermeyer, Uwe; Kula, Maria‐Regina; Wandrey, Christian

doi:10.1111/j.1749-6632.1990.tb18157.x

Cited by 46 publications

(7 citation statements)

References 14 publications

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“…The enhancement of the selectivity of a catalysed main reaction with saturation kinetic in the presence of an undesired uncatalysed first-order side reaction has been studied by Wandrey et al [30]. They concluded that the discrimination of the side reaction is high if the concentration of the substrate is low.…”

Section: Enzymatic Reduction (Fed-batch)mentioning

confidence: 99%

Chemoenzymatic synthesis of the chiral side-chain of statins: application of an alcohol dehydrogenase catalysed ketone reduction on a large scale

Wolberg

Filho

Bode

et al. 2008

Bioprocess Biosyst Eng

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The chemoenzymatic synthesis of the tert-butyl (S)-6-chloro-5-hydroxy-3-ketohexanoate is described. Our approach relies on a highly regio- and enantioselective reduction of a beta,delta-diketohexanoate ester catalysed by NADP(H)-dependent alcohol dehydrogenase of Lactobacillus brevis (LBADH). A detailed description of the scale-up of the enzymatic synthesis of the hydroxyketo ester is given which includes a scale-up of the substrate synthesis as well, i.e. the preparation of diketo ester on a 100 g scale. Furthermore, studies directed towards improving the co-catalyst [NADP(H)] consumption of the enzymatic key step by kinetic studies and application of a biphasic reaction medium were performed.

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Section: Enzymatic Reduction (Fed-batch)mentioning

confidence: 99%

Chemoenzymatic synthesis of the chiral side-chain of statins: application of an alcohol dehydrogenase catalysed ketone reduction on a large scale

Wolberg

Filho

Bode

et al. 2008

Bioprocess Biosyst Eng

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“…The activity of the recombinant isoenzyme PaHNL5 did not change significantly over the range pH 2.5-6.5. PaHNL5 was surprisingly stable under acidic conditions (Figure 1), under which the competitive chemical reaction is suppressed [18,19] and the enantiomerically pure cyanohydrin product is also stable. This extremely important technical feature of HNL reactions in emulsion systems makes the production of pure enantiomers possible even from substrates that react slowly and facilitates effective enzyme recycling.…”

mentioning

confidence: 94%

Comprehensive Step‐by‐Step Engineering of an (R)‐Hydroxynitrile Lyase for Large‐Scale Asymmetric Synthesis

et al. 2003

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“…Finally, the undesired chemically side reaction (non-enzymatic formation of racemic cyanohydrins) can be reduced by decreasing the pH value within the aqueous phase [27,44] or by decreasing the reaction temperature. [28] The mass transfer limitation is also a powerful tool to enhance the enantiomeric excess.…”

Section: Resultsmentioning

confidence: 99%

“…Only small-scale applications, for example, small continuously operated membrane reactors, have proven their practicability under the safety circumstances of hydrogen cyanide. [27] Additionally, a continuous removal of the product (cyanohydrin) is not known so far in enzymatic cyanohydrin synthesis.…”

Section: Resultsmentioning

confidence: 99%

Hydroxynitrile Lyase in Organic Solvent‐Free Systems to Overcome Thermodynamic Limitations

et al. 2007

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Abstract:The overcoming of thermodynamic limitations in the synthesis of optically active ketone cyanohydrins by using organic solvent-free systems has been investigated. Therefore, substrates with known unfavorable results within hydroxynitrile lyase-catalyzed reactions were selected for the determination of limitations and bottlenecks in ketone cyanohydrin synthesis. The highly (S)-selective hydroxynitrile lyase from Manihot esculenta (MeHNL) has been chosen for the conversion of acetophenone and the corresponding derivatives, which are substrates that exhibit only low grades of conversion also with several other hydroxynitrile lyases. With organic solventfree systems under optimized reaction conditions conversions up to 78 % with > 99.0 ee (S) were obtained. Finally, 5 mL of (S)-acetophenone cyanohydrin with an enantiomeric excess of 98.5 % ee (S) were synthesized.

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Engineering Aspects of Enzyme

Cited by 46 publications

References 14 publications

Chemoenzymatic synthesis of the chiral side-chain of statins: application of an alcohol dehydrogenase catalysed ketone reduction on a large scale

Chemoenzymatic synthesis of the chiral side-chain of statins: application of an alcohol dehydrogenase catalysed ketone reduction on a large scale

Comprehensive Step‐by‐Step Engineering of an (R)‐Hydroxynitrile Lyase for Large‐Scale Asymmetric Synthesis

Hydroxynitrile Lyase in Organic Solvent‐Free Systems to Overcome Thermodynamic Limitations

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