Properties of an alcohol dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix K1

Hidehiko Hirakawa, Noriho Kamiya, Yutaka Kawarabayashi, Teruyuki Nagamune

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Abstract

A NAD+-dependent medium-chain alcohol dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix K1 was expressed in Escherichia coli and purified. The recombinant enzyme was a homotetramer of molecular mass 1.6×102 kDa. The optimum pH for the oxidative reaction was around 10.5 and that for the reductive reaction was around 8.0. The enzyme had a broad substrate specificity including aliphatic and aromatic alcohols, aliphatic and aromatic ketones, and benzylaldehyde. This enzyme produced (S)-alcohols from the corresponding ketones. The enzyme was thermophilic and the catalytic activity increased up to 95°C. It maintained 24% of the original catalytic activity after incubation for 30 min at 98°C, indicating that this enzyme is highly thermostable.

Original languageEnglish
Pages (from-to)202-206
Number of pages5
JournalJournal of Bioscience and Bioengineering
Volume97
Issue number3
DOIs
Publication statusPublished - Jan 1 2004

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All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology

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