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Applied and Environmental Microbiology, October 2001, p. 4546-4553, Vol. 67, No. 10
0099-2240/01/$04.00+0   DOI: 10.1128/AEM.67.10.4546-4553.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Physiological Role of beta -Phosphoglucomutase in Lactococcus lactis

Fredrik Levander, Ulrika Andersson, and Peter Rådström*

Applied Microbiology, Center for Chemistry and Chemical Engineering, Lund Institute of Technology, Lund University, SE-221 00 Lund, Sweden

Received 8 January 2001/Accepted 26 April 2001

A beta -phosphoglucomutase (beta -PGM) mutant of Lactococcus lactis subsp. lactis ATCC 19435 was constructed using a minimal integration vector and double-crossover recombination. The mutant and the wild-type strain were grown under controlled conditions with different sugars to elucidate the role of beta -PGM in carbohydrate catabolism and anabolism. The mutation did not significantly affect growth, product formation, or cell composition when glucose or lactose was used as the carbon source. With maltose or trehalose as the carbon source the wild-type strain had a maximum specific growth rate of 0.5 h-1, while the deletion of beta -PGM resulted in a maximum specific growth rate of 0.05 h-1 on maltose and no growth at all on trehalose. Growth of the mutant strain on maltose resulted in smaller amounts of lactate but more formate, acetate, and ethanol, and approximately 1/10 of the maltose was found as beta -glucose 1-phosphate in the medium. Furthermore, the beta -PGM mutant cells grown on maltose were considerably larger and accumulated polysaccharides which consisted of alpha -1,4-bound glucose units. When the cells were grown at a low dilution rate in a glucose and maltose mixture, the wild-type strain exhibited a higher carbohydrate content than when grown at higher growth rates, but still this content was lower than that in the beta -PGM mutant. In addition, significant differences in the initial metabolism of maltose and trehalose were found, and cell extracts did not digest free trehalose but only trehalose 6-phosphate, which yielded beta -glucose 1-phosphate and glucose 6-phosphate. This demonstrates the presence of a novel enzymatic pathway for trehalose different from that of maltose metabolism in L. lactis.

* Corresponding author. Mailing address: Applied Microbiology, Center for Chemistry and Chemical Engineering, Lund Institute of Technology, Lund University, P.O. Box 124, SE-221 00 Lund, Sweden. Phone: 46 46 222 3412. Fax: 46 46 222 4203. E-mail: Peter.Radstrom{at}tmb.lth.se.

Applied and Environmental Microbiology, October 2001, p. 4546-4553, Vol. 67, No. 10
0099-2240/01/$04.00+0   DOI: 10.1128/AEM.67.10.4546-4553.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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