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Applied and Environmental Microbiology, February 2006, p. 1402-1409, Vol. 72, No. 2
0099-2240/06/$08.00+0 doi:10.1128/AEM.72.2.1402-1409.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Institut National de la Recherche Agronomique, Unité de Biochimie et Structure des Protéines, 78352 Jouy en Josas, France,1 R & D Fromageries Bel, Vendôme, France2
Received 15 September 2005/ Accepted 12 December 2005
Amino acid conversion to aroma compounds by Lactococcus lactis is limited by the low production of
-ketoglutarate that is necessary for the first step of conversion. Recently, glutamate dehydrogenase (GDH) activity that catalyzes the reversible glutamate deamination to
-ketoglutarate was detected in L. lactis strains isolated from a vegetal source, and the gene responsible for the activity in L. lactis NCDO1867 was identified and characterized. The gene is located on a 70-kb plasmid also encoding cadmium resistance. In this study, gdh gene inactivation and overexpression confirmed the direct impact of GDH activity of L. lactis on amino acid catabolism in a reaction medium at pH 5.5, the pH of cheese. By using cadmium resistance as a selectable marker, the plasmid carrying gdh was naturally transmitted to another L. lactis strain by a mating procedure. The transfer conferred to the host strain GDH activity and the ability to catabolize amino acids in the presence of glutamate in the reaction medium. However, the plasmid appeared unstable in a strain also containing the protease lactose plasmid pLP712, indicating an incompatibility between these two plasmids.
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