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

Journal Article · Thu Dec 31 04:00:00 EST 1992 · Applied Microbiology and Biotechnology

DOI:https://doi.org/10.1007/BF00180975· OSTI ID:625679

Bryant, F O; Ljungdahl, L G; Wiegel, J ^[1]

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1. Univ. of Georgia, Athens, GA (United States)

A mutant strain of `Thermoanaerobacter ethanolicus` (ATCC 31550) designated JW200 Fe 4 contains primary and secondary alcohol dehydrogenases (ADHs). The primary ADH from JW200 Fe 4 was formed early in the growth cycle compared to the primary ADH from 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 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.

• Sponsoring Organization: USDOE
• DOE Contract Number: AS09-79ER10499
• OSTI ID: 625679
• Journal Information: Applied Microbiology and Biotechnology, Journal Name: Applied Microbiology and Biotechnology Vol. 37; ISSN AMBIDG; ISSN 0175-7598
• Country of Publication: Germany
• Language: English

Related Subjects

55 BIOLOGY AND MEDICINE
BASIC STUDIES
ACETALDEHYDE
ALCOHOL DEHYDROGENASE
ELECTROPHORESIS
ETHANOL
MUTANTS