Conversion of phenylpyruvate to l-phenylalanine by immobilized Clostridium butyricum-alanine dehydrogenase-Micrococcus luteus under hydrogen high pressure

Tadashi Matsunaga, M. Higashijima, H. Nakatsugawa, S. Nishimura, T. Kitamura, M. Tsuji, T. Kawaguchi

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

Alanine was the best amino donor among various amino acids and NH4Cl for the phenylalanine production of Micrococus luteus. l-Alanine was regenerated at the rate of 9.2μ moles/min/g dry cells from NH4Cl and pyruvate by immobilized Clostridium butyricum-alanine dehydrogenase. l-Phenylalanine was continuously produced from hydrogen, NH4Cl and phenylpyruvate by coupling immobilized C. butyricum, alanine dehydrogenase and M. luteus. The rate of phenylalanine production was 1.74 μ moles/min/g dry cells.

Original languageEnglish
Pages (from-to)11-14
Number of pages4
JournalApplied Microbiology and Biotechnology
Volume27
Issue number1
DOIs
Publication statusPublished - 1987 Oct
Externally publishedYes

Fingerprint

Alanine Dehydrogenase
Clostridium butyricum
Micrococcus luteus
Phenylalanine
Hydrogen
Pressure
Alanine
Pyruvic Acid
Amino Acids
phenylpyruvic acid

ASJC Scopus subject areas

  • Biotechnology
  • Applied Microbiology and Biotechnology

Cite this

Conversion of phenylpyruvate to l-phenylalanine by immobilized Clostridium butyricum-alanine dehydrogenase-Micrococcus luteus under hydrogen high pressure. / Matsunaga, Tadashi; Higashijima, M.; Nakatsugawa, H.; Nishimura, S.; Kitamura, T.; Tsuji, M.; Kawaguchi, T.

In: Applied Microbiology and Biotechnology, Vol. 27, No. 1, 10.1987, p. 11-14.

Research output: Contribution to journalArticle

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AU - Tsuji, M.

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