Summary
For production of l-phenylalanine the reductive amination of phenylpyruvate, catalyzed by phenylalanine-dehydrogenase was examined. To reach high levels and a sufficient stability of the inducible intracellular enzyme, growth conditions of Brevibacterium sp. are optimized. For continuous production of l-phenylalanine in an enzyme membrane reactor, the kinetic parameters of the partially purified enzyme are determined.
In continuous production a space time yield of 37.4 g l-Phe l-1 d-1 can be reached.
By means of the measured kinetic parameters and simultaneous calculation of the mass balances of all reaction components the behaviour of the reactor can be simulated. For certain conditions the multi-enzyme-system shows multiple steady-states.
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Abbreviations
- l-phe:
-
l-phenylalanine
- phepy:
-
phenylpyruvate
- PEG:
-
polyethylenglycol
- pheDH:
-
l-phenylalanine dehydrogenase
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Hummel, W., Schmidt, E., Wandrey, C. et al. l-Phenylalanine dehydrogenase from Brevibacterium sp. for production of l-phenylalanine by reductive amination of phenylpyruvate. Appl Microbiol Biotechnol 25, 175–185 (1986). https://doi.org/10.1007/BF00253645
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DOI: https://doi.org/10.1007/BF00253645