Abstract

Enzyme catalyzed reactions are complex reactions due to the interplay of the enzyme, the reactants, and the operating conditions. To handle this complexity systematically and make use of a design space without technical restrictions, we apply the model based approach of elementary process functions (EPF) for selecting the best process design for enzyme catalysis problems. As a representative case study, we consider the carboligation of propanal and benzaldehyde catalyzed by benzaldehyde lyase from Pseudomonas fluorescens (PfBAL) to produce (R)-2-hydroxy-1-phenylbutan-1-one, because of the substrate dependent reaction rates and the challenging substrate dependent PfBAL inactivation. The apparatus independent EPF concept optimizes the material fluxes influencing the enzyme catalyzed reaction for the given process intensification scenarios. The final product concentration is improved by 13% with the optimized feeding rates, and the optimization results are verified experimentally. In general, the rigorous model driven approach could lead to selecting the best existing reactor, designing novel reactors for enzyme catalysis, and combining protein engineering and process systems engineering concepts.

Highlights

  • The pharmaceutical industry is considering biocatalytic processes as a possible alternative to chemocatalytic processes [1,2,3]

  • Following the elementary process functions (EPF) strategy, three intensification cases were investigated systematically to ascertain the best process intensification scenario for the maximization of the final concentration of (R)-2-hydroxy-1-phenylbutan-1-one produced from the Pf BAL catalyzed carboligation between propanal and benzaldehyde

  • Catalyzed cross-carboligation of benzaldehyde and propanal, the final concentration of the product (R)-2-hydroxy-1-phenylbutan-1-one was chosen as the objective function to be optimized, and three process intensification scenarios were evaluated making use of the EPF concept

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Summary

Introduction

The pharmaceutical industry is considering biocatalytic processes as a possible alternative to chemocatalytic processes [1,2,3] This is primarily due to the high stereoselectivity and specificity of biocatalytic processes, which lead to efficient production of high-quality active pharmaceutical ingredients (APIs) in fewer synthesis steps [2,3]. To render enzyme processes economically viable, a high product concentration and low enzyme cost must be ensured [2]. To this end, the advancements in protein engineering [1], appropriate reaction engineering concepts [4], and process intensification strategies must be combined [5,6]. As examples of the application of model based approaches to Catalysts 2020, 10, 96; doi:10.3390/catal10010096 www.mdpi.com/journal/catalysts

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