Abstract
Flow processes and enzyme immobilization have gained much attention over the past few years in the field of biocatalytic process design. Downstream processes and enzyme stability can be immensely simplified and improved. In this work, we report the utilization of polymer network-entrapped enzymes and their applicability in flow processes. We focused on the superabsorber-based immobilization of an alcohol dehydrogenase (ADH) from Lactobacillus brevis and its application for a reduction of acetophenone. The applicability of this immobilization technique for a biotransformation running in a packed bed reactor was then demonstrated. Towards this end, the immobilized system was intensively studied, first in a batch mode, leading to >90% conversion within 24 h under optimized conditions. A subsequent transfer of this method into a flow process was conducted, resulting in very high initial conversions of up to 67% in such a continuously running process.
Highlights
The development of flow processes has gained tremendous interest in recent years in organic chemistry due to numerous advantages of such types of processes over classic batch approaches [1]
We report the utilization of polymer network-entrapped enzymes and their applicability in flow processes
We focused on the superabsorber-based immobilization of an alcohol dehydrogenase (ADH) from Lactobacillus brevis and its application for a reduction of acetophenone
Summary
The development of flow processes has gained tremendous interest in recent years in organic chemistry due to numerous advantages of such types of processes over classic batch approaches [1]. An increasing number of examples of biocatalysis in flow processes have been reported [22,23,24,25,26,27]. Only being studied to a minor extent, some examples of ketone reductions with an alcohol dehydrogenase (ADH) in flow processes have been described [28,29,30,31,32,33,34]. Our group published an improved downstream process by means of such a segmented flow process, illustrated using two different ADHs and substrates [34]
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