l-Phenylalanine dehydrogenase from Brevibacterium sp. for production of l-phenylalanine by reductive amination of phenylpyruvate |
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Authors: | Werner Hummel Elke Schmidt Christian Wandrey Maria-Regina Kula |
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Institution: | (1) Gesellschaft für Biotechnologische Forschung, D-3300 Braunschweig, Germany;(2) Institut für Biotechnologie der KFA Jülich, D-5170 Jülich, Germany;(3) Present address: Institut für Enzymtechnologie der Universität Düsseldorf in der KFA Jülich, D-5170 Jülich, Germany;(4) Institut für Enzymtechnologie der Universität Düsseldorf, in der KFA Jülich, Postfach 2050, D-5170 Jülich, Germany |
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Abstract: | 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.Abbreviations
l-phe
l-phenylalanine
- phepy
phenylpyruvate
- PEG
polyethylenglycol
- pheDH
l-phenylalanine dehydrogenase |
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