Production of D-Glutamate from L-Glutamate with Glutamate Racemase and L-Glutamate Oxidase.
Biosci Biotechnol Biochem
; 63(12): 2168-73, 1999.
Article
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| MEDLINE
| ID: mdl-27373918
ABSTRACT
We studied production of D-glutamate from L-glutamate using a bioreactor consisting of two columns of sequentially connected immobilized glutamate racemase (EC 5.1.1.3, from Bacillus subtilis IFO 3336) and L-glutamate oxidase (EC 1.4.3.11, from Streptomyces sp. X119-6) L-glutamate was racemized by the glutamate racemase column, and then L-glutamate was oxidized by the L-glutamate oxidase column. Consequently only D-glutamate remained, and was easily separated from the α-ketoglutarate formed by anion-exchange chromatography. Both enzymes were highly stabilized by immobilization. The pH and temperature optima of immobilized glutamate racemase (pH 8, 40°C) were similar to those of immobilized L-glutamate oxidase (pH 7, 50°C). Accordingly, we connected the two columns tandemly to do both enzyme reactions under the same conditions. Actually 4.5 µmol of D-glutamate was produced and isolated from 10 µmol of L-glutamate, about 90% of the theoretical yield.
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1
Colección:
01-internacional
Base de datos:
MEDLINE
Idioma:
En
Revista:
Biosci Biotechnol Biochem
Asunto de la revista:
BIOQUIMICA
/
BIOTECNOLOGIA
Año:
1999
Tipo del documento:
Article