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J Bacteriol, June 1998, p. 3049-3055, Vol. 180, No. 12
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Cloning of the Lactococcus lactis adhE
Gene, Encoding a Multifunctional Alcohol Dehydrogenase, by
Complementation of a Fermentative Mutant of Escherichia
coli
José
Arnau,*
Flemming
Jørgensen,
Søren M.
Madsen,
Astrid
Vrang, and
Hans
Israelsen
Biotechnological Institute, DK-2970
Hørsholm, Denmark
Received 21 December 1997/Accepted 8 April 1998
The Lactococcus lactis adhE gene, which encodes a
multifunctional alcohol dehydrogenase, has been cloned and
characterized. A DNA fragment encoding the putative alcohol
dehydrogenase domain of the AdhE protein was cloned by screening an
L. lactis genomic library in a fermentative mutant of
Escherichia coli and selecting for the ability to grow
anaerobically. Further analysis of the clone obtained allowed the
cloning of the entire adhE gene sequence. Analysis of
adhE expression in L. lactis during
anaerobiosis showed induction at the transcriptional level, especially
in medium containing glucose. Constructed mutant strains produced
reduced amounts of ethanol under anaerobic conditions. With the
L. lactis gene as a probe, adhE homologs were
found in other industrially relevant lactic acid bacteria.
*
Corresponding author. Mailing address: Biotechnological
Institute, Kogle Allé 2, DK-2970 Hørsholm, Denmark. Phone: 45 45 16 04 44. Fax: 45 45 16 04 55. E-mail: arnau{at}biobase.dk.
J Bacteriol, June 1998, p. 3049-3055, Vol. 180, No. 12
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
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