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  • Author or Editor: László Poppe x
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The lipase catalyzed 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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Biotransformation of l-phenylalanine (l-1a) and five unnatural substrates (rac-1bf) by phenylalanine ammonia-lyase (PAL) was investigated in a novel microfluidic device (Magne-Chip) that comprises microliter volume reaction cells filled with PAL-coated magnetic nanoparticles (MNPs). Experiments proved the excellent reproducibility of enzymecatalyzed biotransformation in the chip and the excellent reusability of the enzyme layer during 14 h continuous measurement (>98% over 7 repetitive measurements with l-1a). The platform also enabled fully automatic multiparameter measurements with a single biocatalyst loading of about 1 mg PAL-MNP. Computational fluid dynamics (CFD) calculations were used to study the flow field in the chambers and the effect of unintended bubble formation. Optimal flow rate for l-1a reaction and specific activities for rac-1bf under these conditions were determined.

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