Abstract
To choose the most effective process design in enzyme process development it is important to find the most effective reactor mode of operation. This goal is achieved by modeling of the reaction kinetics as a tool of enzyme reaction engineering. With the example of the transketolase catalyzed L-erythrulose synthesis we demonstrate how the most effective reactor mode can be determined by kinetic simulations. This is of major importance if the biocatalyst deactivation is caused by one of the substrates as in this case by glycolaldehyde. The cascade of two membrane reactors in series with soluble enzyme is proposed as a solution for the enzyme deactivation by one of the substrates.
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Acknowledgements
The authors gratefully acknowledge financial support from Deutsche Forschungsgemeinschaft: SFB 380 "Asymmetric synthesis with chemical and biological methods" TP B21 and C1, for part of this work.
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Vasic-Racki, D., Bongs, J., Schörken, U. et al. Modeling of reaction kinetics for reactor selection in the case of L-erythrulose synthesis. Bioprocess Biosyst Eng 25, 285–290 (2003). https://doi.org/10.1007/s00449-002-0312-y
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DOI: https://doi.org/10.1007/s00449-002-0312-y