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The highly stable alcohol dehydrogenase of Thermomicrobium roseum: purification and molecular characterization
- Issue Date
- Jun-2002
- Publisher
- PERGAMON-ELSEVIER SCIENCE LTD
- Keywords
- alcohol dehydrogenase; thermophilic bacterium; enzymatic characterization; homo-dimer; N-terminal amino acid sequence; purification; stability; substrate specificity; Thermomicrobium roseum
- Citation
- COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY, v.132, no.2, pp 415 - 422
- Pages
- 8
- Journal Title
- COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY
- Volume
- 132
- Number
- 2
- Start Page
- 415
- End Page
- 422
- ISSN
- 1096-4959
1879-1107
- Abstract
- An alcohol dehydrogenase (ADH) was purified to electrophoretic homogeneity from an extremely thermophilic bacterium, Thermomicrobium roseum. The native enzyme was found to be a homo-dimer of 43-kDa subunits. The pI of the enzyme was determined to be 6.2, while its optimum pH is 10.0. The enzyme oxidized mainly primary aliphatic alcohols and exhibited high substrate specificity towards ethanol, n-propanol and crotyl alcohol. The highest reaction rate was observed when ethanol was used as substrate and the Km value of the enzyme for ethanol was 24.2 mM. Pyrazole notably inhibited the enzymatic activity. The enzyme had the optimal temperature of 70 degreesC and was highly stable against high temperature. (C) 2002 Elsevier Science Inc. All rights reserved.
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