Multipurpose fixed-bed bioreactor to simplify lipase production by solid-state fermentation and application in biocatalysis

One-pot synthesis of (R)-2-acetoxy-1-indanone from 1,2-indanedione combining metal catalyzed hydrogenation and chemoenzymatic dynamic kinetic resolution

Enzymatic kinetic resolution of racemic 1-phenylethanol catalysed by immobilized Candida antarctica lipase B was investigated in a neat system at the temperature range of 30–70 °C. Synthetic triglycerides, namely glycerol triacetate and glycerol tributyrate, were applied as the esterification agents. Both esterification agents were efficient regarding to the enantioselectivity (>1000). Initial rate of reaction and the kinetic constants were influenced by the applied esterification agent significantly. A detailed modelling approach is presented and verified in the temperature range on 30–60 °C for the tributyrin system.

/pdf/neat-lipase-catalysed-kinetic-resolution-of-racemic-1-4xtbzku1dz.pdf

Neat lipase-catalysed kinetic resolution of racemic 1-phenylethanol and a straightforward modelling of the reaction

This chapter demonstrates with a wide range of examples the high potential of continuous-flow techniques for stereoselective biotransformations catalyzed by enzymes, especially hydrolases. Benefits of the various reactor setups are discussed, for example, the continuous flow packed bed reactors can enhance the productivity of enzyme-catalyzed processes or miniaturized continuous flow systems allow fast high-throughput screenings. Continuous flow microreactor systems enabled integration of enzyme-catalysis with chemical steps (e.g., in dynamic kinetic resolutions) or with continuous extraction or performing multienzyme-catalyzed multistep biotransformations. Thus, the potential of continuous-flow microreactor systems with immobilized biocatalysts is demonstrated as process development tool for stereoselective biotransformations.

Stereoselective Hydrolase‐Catalyzed Processes in Continuous‐Flow Mode

Comparative assessment of characteristics of industrial and laboratory highly-efficient samples of adsorbents-desiccants

The kinetic resolution of racemic 1-phenylethanol with ethyl acetate was investigated in a down-flow fixed-bed reactor operated in a continuous mode mainly at the molar ratio of 1: 3 in 400 mL toluene at 70°C. The catalytic activity of the immobilized lipase was studied by: (i) changing the flow rates, (ii) utilizing different substrate concentrations, (iii) applying step changes using ethyl acetate, ethyl benzene, acetic acid, acetophenone etc., (iv) investigating the inhibitory effect of either the desired or the stoichiometric products (R)-1-phenylethyl acetate and ethanol, respectively), (v) elucidating the effect of water on the activity and stability of the immobilized lipase. The residence time distribution and the reactor hydrodynamics were also discussed along with kinetic modelling. The results were linked to the one-pot reactions.

Lipase-catalyzed acylation in a continuous down-flow fixed-bed reactor

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Lipase-catalyzed acylation in a continuous down-flow fixed-bed reactor