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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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