Purification and some characteristics of a monomeric alanine racemase from an extreme thermophile, Thermus thermophilus

Kenji Inagaki, Kenji Inagaki, Takeshi Nakamura, Takashi Tamura, Takashi Tamura, Hidehiko Tanaka

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15 Citations (Scopus)


We purified to homogeneity an alanine racemase (EC from Thermus thermophilus HB8, an extreme thermophile. Interestingly, the enzyme possessed a monomeric structure with a molecular weight of about 38,000. The enzyme was most active at pH 8 and 75°C, and remained active after incubation at 80°C for 30 min.

Original languageEnglish
Pages (from-to)344-346
Number of pages3
JournalJournal of Bioscience and Bioengineering
Issue number3
Publication statusPublished - Sep 2000



  • Alanine racemase
  • Extreme thermophile
  • Thermus thermophilus

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering

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