Applied Microbiology and Biotechnology

, Volume 26, Issue 5, pp 409–416

Isolation of l-phenylalanine dehydrogenase from Rhodococcus sp. M4 and its application for the production of l-phenylalanine

  • Werner Hummel
  • Horst Schütte
  • Elke Schmidt
  • Christian Wandrey
  • Maria-Regina Kula
Biotechnology

DOI: 10.1007/BF00253523

Cite this article as:
Hummel, W., Schütte, H., Schmidt, E. et al. Appl Microbiol Biotechnol (1987) 26: 409. doi:10.1007/BF00253523

Summary

l-Phenylalanine dehydrogenase [l-phenylalanine: NAD+-oxidoreductase (deaminating)] of Rhodococcus sp. strain M4 was studied emphasizing its application for the production of l-phenylalanine. A high enzyme level (30,000 U·l-1, 25–30 U·mg-1 in the crude extract) could be reached during aerob degradation of l-phenylalanine (10 g·l-1) under optimized growth coditions. A partial purification of the intracellular enzyme by liquid-liquid extraction, and DEAE-cellulose led to a specific activity of more than 1300 U·mg-1. The continuous production of l-phenylalanine in an enzyme-membrane-reactor for 350h resulted in a space-time yield of 456 g·l-1·d-1 with a mean substrate conversion of 95%. Consumption of phenylalanine dehydrogenase was 1,500 U·kg Phe-1.

Abbreviations

BSA

bovine serum albumine

pheDH

l-phenylalanine dehydrogenase

phepyr

phenylpyruvate

OD

optical density

FDH

formate dehydrogenase

Copyright information

© Springer-Verlag 1987

Authors and Affiliations

  • Werner Hummel
    • 1
  • Horst Schütte
    • 1
  • Elke Schmidt
    • 2
  • Christian Wandrey
    • 2
  • Maria-Regina Kula
    • 1
  1. 1.Gesellschaft für Biotechnologische ForschungBraunschweigFederal Republic of Germany
  2. 2.Institut für Biotechnologie der KFA JülichJülichFederal Republic of Germany
  3. 3.Institut für Enzymtechnologie der Universität Düsseldorf in der KFA JülichJülichFederal Republic of Germany
  4. 4.Institut für Enzymtechnologie der Universität Düsseldorf in der KFA JülichJülichFRG

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