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Applied and Environmental Microbiology, December 2006, p. 7933-7940, Vol. 72, No. 12
0099-2240/06/$08.00+0 doi:10.1128/AEM.00659-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
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Lidia Muscariello,2
Frederique Lorquet,1,
Aline Stukkens,1
Deborah Prozzi,1
Margherita Sacco,2
Michiel Kleerebezem,3 and
Pascal Hols1*
Unité de Génétique, Institut des Sciences de la Vie, Université Catholique de Louvain, Croix du Sud 5, B-1348 Louvain-la-Neuve, Belgium,1 Dipartimento di Scienze Ambientali, Seconda Università di Napoli, Via Vivaldi 43, 81100 Caserta, Italy,2 Wageningen Centre for Food Sciences, NIZO food research, P.O. Box 20, 6710 BA Ede, The Netherlands3
Received 22 March 2006/ Accepted 25 September 2006
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 oxidase activity under the tested conditions. We show here that L. plantarum has two major pyruvate oxidases: PoxB and PoxF. Both are involved in lactate-to-acetate conversion in the 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, with lactate remaining the major end product of either glucose or maltose fermentation. Notably, survival during the stationary phase appeared to be dramatically improved in the poxB poxF double mutant.
Published ahead of print on 29 September 2006.
Supplemental material for this article may be found at http://aem.asm.org/.
Present address: Wageningen Centre for Food Sciences, NIZO food research, PO Box 20, 6710 BA Ede, The Netherlands.
Present address: Génétique Microbienne, INRA, 78352 Jouy en Josas Cedex, France.
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