Abstract
Phenylalanine was produced from phenylpyruvate at up to 30 g/l in molar yields as high as 98% using polyazetidine immobilized E. coli high in aspartate phenylalanine transaminase. E. coli mutants containing only the tyrosine phenylalanine transaminase (tyrB) or the branched chain transaminase (ilvE) were unable to convert phenylpyruvate to phenylalanine at high levels. Aspartic acid was the amine donor of choice as the oxaloacetic acid produced in the reaction was readily decarboxylated to pyruvic acid under the experimental conditions thereby driving the reaction to completion. The catalyst had a projected half–life of greater than 8 months at temperatures of 37–41°C.
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Calton, G., Wood, L., Updike, M. et al. The Production of L–Phenylalanine by Polyazetidine Immobilized Microbes. Nat Biotechnol 4, 317–320 (1986). https://doi.org/10.1038/nbt0486-317
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DOI: https://doi.org/10.1038/nbt0486-317
