Isolation of l-phenylalanine dehydrogenase from Rhodococcus sp. M4 and its application for the production of l-phenylalanine |
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Authors: | Werner Hummel Horst Schütte Elke Schmidt Christian Wandrey Maria-Regina Kula |
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Affiliation: | (1) Gesellschaft für Biotechnologische Forschung, D-3300 Braunschweig, Federal Republic of Germany;(2) Institut für Biotechnologie der KFA Jülich, D-5170 Jülich, Federal Republic of Germany;(3) Present address: Institut für Enzymtechnologie der Universität Düsseldorf in der KFA Jülich, D-5170 Jülich, Federal Republic of Germany;(4) Institut für Enzymtechnologie der Universität Düsseldorf in der KFA Jülich, PO 20 50, D-5170 Jülich, FRG |
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Abstract: | 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 |
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