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 language | English |
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Pages (from-to) | 202-206 |
Number of pages | 5 |
Journal | Journal of Bioscience and Bioengineering |
Volume | 97 |
Issue number | 3 |
DOIs | |
Publication status | Published - Jan 1 2004 |
All Science Journal Classification (ASJC) codes
- Biotechnology
- Bioengineering
- Applied Microbiology and Biotechnology