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AEM Accepts, published online ahead of print on 29 September 2006
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Appl. Environ. Microbiol. doi:10.1128/AEM.00659-06
Copyright (c) 2006, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Involvement of pyruvate oxidase activity and acetate production in the survival of Lactobacillus plantarum during the stationary phase of aerobic growth

PHILIPPE GOFFIN, LIDIA MUSCARIELLO, FREDERIQUE LORQUET, ALINE STUKKENS, DEBORAH PROZZI, MARGHERITA SACCO, MICHIEL KLEEREBEZEM, and PASCAL HOLS*

Unité de Génétique, Institut des Sciences de la Vie, Université catholique de Louvain, Croix du Sud 5, B-1348 Louvain-la-Neuve, Belgium, Dipartimento di Scienze Ambientali, Seconda Università di Napoli, via Vivaldi 43, 81100, Caserta, Italy, and Wageningen Centre for Food Sciences; NIZO food research, PO Box 20, 6710 BA, Ede, The Netherlands

* To whom correspondence should be addressed. Email: hols{at}gene.ucl.ac.be.


   Abstract

In addition to the previously characterized pyruvate oxidase PoxB, the Lactobacillus plantarum genome encodes four predicted pyruvate oxidases (PoxC, PoxD, PoxE and PoxF). Each pyruvate oxidase gene was individually inactivated and only the knockout of poxF resulted in a decrease in pyruvate activity under the tested conditions. Here, we show that L. plantarum has two major pyruvate oxidases, PoxB and PoxF. Both are involved in lactate-to-acetate conversion in early stationary phase of aerobic growth and are regulated by carbon catabolite repression. A strain devoid of pyruvate oxidase activity was constructed by knocking out the poxB and poxF genes. In this mutant, acetate production was strongly affected, lactate remaining the major end product of either glucose or maltose fermentation. Notably, survival during stationary phase appeared to be dramatically improved in the poxB poxF double mutant.




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