4.6 Review

Getting the Most Out of Enzyme Cascades: Strategies to Optimize In Vitro Multi-Enzymatic Reactions

Journal

CATALYSTS
Volume 11, Issue 10, Pages -

Publisher

MDPI
DOI: 10.3390/catal11101183

Keywords

biocatalysis; in vitro biotransformation; one-pot process; multi-enzymatic reactions; enzyme cascade; cascade optimization; kinetic modelling

Funding

  1. European Research Council (ERC) [757320]
  2. Deutsche Forschungsgemeinschaft (DFG) [445751305]
  3. [SPP 2240]
  4. European Research Council (ERC) [757320] Funding Source: European Research Council (ERC)

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In vitro enzyme cascades have advantages such as strong synthetic capabilities and no need for intermediate isolation, but their performance can be influenced by various factors. Optimizing these systems is essential yet challenging.
In vitro enzyme cascades possess great benefits, such as their synthetic capabilities for complex molecules, no need for intermediate isolation, and the shift of unfavorable equilibria towards the products. Their performance, however, can be impaired by, for example, destabilizing or inhibitory interactions between the cascade components or incongruous reaction conditions. The optimization of such systems is therefore often inevitable but not an easy task. Many parameters such as the design of the synthesis route, the choice of enzymes, reaction conditions, or process design can alter the performance of an in vitro enzymatic cascade. Many strategies to tackle this complex task exist, ranging from experimental to in silico approaches and combinations of both. This review collates examples of various optimization strategies and their success. The feasibility of optimization goals, the influence of certain parameters and the usage of algorithm-based optimizations are discussed.

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