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Journal of Bacteriology, August 1999, p. 4768-4773, Vol. 181, No. 16
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Transport of D-Xylose in Lactobacillus pentosus, Lactobacillus casei, and Lactobacillus plantarum: Evidence for a Mechanism of Facilitated Diffusion via the Phosphoenolpyruvate:Mannose Phosphotransferase System

Stéphane Chaillou,1,2 Peter H. Pouwels,1,2,* and Pieter W. Postma1

EC Slater Institute, BioCentrum, University of Amsterdam, 1018 TV Amsterdam,1 and Department of Molecular Genetics and Gene Technology, TNO Nutrition and Food Research Institute, 3700AJ Zeist,2 The Netherlands

Received 4 November 1998/Accepted 10 June 1999

We have identified and characterized the D-xylose transport system of Lactobacillus pentosus. Uptake of D-xylose was not driven by the proton motive force generated by malolactic fermentation and required D-xylose metabolism. The kinetics of D-xylose transport were indicative of a low-affinity facilitated-diffusion system with an apparent Km of 8.5 mM and a Vmax of 23 nmol min-1 mg of dry weight-1. In two mutants of L. pentosus defective in the phosphoenolpyruvate:mannose phosphotransferase system, growth on D-xylose was absent due to the lack of D-xylose transport. However, transport of the pentose was not totally abolished in a third mutant, which could be complemented after expression of the L. curvatus manB gene encoding the cytoplasmic EIIBMan component of the EIIMan complex. The EIIMan complex is also involved in D-xylose transport in L. casei ATCC 393 and L. plantarum 80. These two species could transport and metabolize D-xylose after transformation with plasmids which expressed the D-xylose-catabolizing genes of L. pentosus, xylAB. L. casei and L. plantarum mutants resistant to 2-deoxy-D-glucose were defective in EIIMan activity and were unable to transport D-xylose when transformed with plasmids containing the xylAB genes. Finally, transport of D-xylose was found to be the rate-limiting step in the growth of L. pentosus and of L. plantarum and L. casei ATCC 393 containing plasmids coding for the D-xylose-catabolic enzymes, since the doubling time of these bacteria on D-xylose was proportional to the level of EIIMan activity.

* Corresponding author. Mailing address: Department of Molecular Genetics and Gene Technology, TNO Nutrition and Food Research Institute, P.O. Box 360, 3700 AJ Zeist, The Netherlands. Phone: 31 30 6944 462. Fax: 31 30 6944 466. E-mail: Pouwels{at}voeding.tno.nl.

Journal of Bacteriology, August 1999, p. 4768-4773, Vol. 181, No. 16
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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