Comparison of alcohol dehydrogenases from wild-type and mutant strain, JW200 Fe 4, of ‘Thermoanaerobacter ethanolicus’

Autor: Bryant, Frank O., Wiegel, Juergen, Ljungdahl, Lars G.
Zdroj: Applied Microbiology and Biotechnology; July 1992, Vol. 37 Issue: 4 p490-495, 6p
Abstrakt: A mutant strain of ‘Thermoanaerobacter ethanolicus’ (ATCC 31 550) designated JW200 Fe 4 contains primary and secondary alcohol dehydrogenases (ADHs). The primary ADH from JW000 Fe 4 was formed early in the growth cycle compared to the primary ADH form the wild-type strain (JW200 wt). The secondary ADH displayed 2.5-fold greater activity during the growth cycle of JW200 Fe 4 compared to the secondary ADH form JW200 wt. Both primary and secondary ADHs from JW200 Fe 4 were purified to homogeneity ADHs from JW200 Fe 4 were purified to homogeneity as determined by sodium dodecyl sulphate-gel electrophoresis. Relative molecular weight estimations indicated that both ADHs were tetrameric. Each ADH from JW200 Fe 4 contained approximately four Zn atoms per subunit and displayed Arrhenius plots similar to the ADHs from JW200 wt. The substrate specificity for the ADHs from JW200 Fe 4 was similar to that of the ADHs from JW200 wt. The secondary ADH oxidized 2-propanol at 51 times the rate of ethanol. Both ADHs from JW200 Fe 4 apparently reduce acetaldehyde to ethanol while only the secondary ADH from JW200 wt was suggested to contribute significantly to ethanol production.
Databáze: Supplemental Index