|
|
||||||||
1Department of Applied Microbiology, Lund Institute of Technology, Lund University, PO Box 124, S-221 00 Lund, Sweden
2Department of Food Technology, Victoria University, PO Box 14428, MCMC Melbourne, Victoria 8001, Australia
ABSTRACT
Maltose metabolism in Lactococcus lactis involves the conversion of β-glucose 1-phosphate to glucose 6-phosphate, a reaction which is reversibly catalysed by a maltose-inducible and glucose-repressible β-phosphoglucomutase (β-PGM). The gene encoding β-PGM (pgmB) was cloned from a genomic library of L. lactis using antibodies. The nucleotide sequence of a 5695 bp fragment was determined and six ORFs, including the pgmB gene, were found. The gene expressed a polypeptide with a calculated molecular mass of 24210 Da, which is in agreement with the molecular mass of the purified β-PGM (25 kDa). A short sequence at the N-terminus was found to be similar to known metal-binding domains. The expression of β-PGM in L. lactis was found to be induced also by trehalose and sucrose, and repressed by lactose in the growth medium. This indicates that β-PGM does not serve solely to degrade maltose, but that it is also involved in the metabolism of other carbohydrates. The specific activity of
-PGM during fermentation was dependent on the maltose concentration in the medium. The maximum specific activity of β-PGM increased by a factor of 4.6, and the specific growth rate by a factor of 7, when the maltose concentration was raised from 0.8 to 11.0 g I-1. Furthermore, a higher amount of lactate produced relative to formate, acetate and ethanol was observed when the initial maltose concentration in the medium was increased. The specific activity of β-PGM responded similarly to β-PGM, but the magnitude of the response was lower. Preferential sugar utilization and
- and β-PGM suppression was observed when L. lactis was grown on the substrate combinations glucose and maltose, or lactose and maltose; maltose was the least-preferred sugar. In contrast, galactose and maltose were utilized concurrently and both PGM activities were high throughout the fermentation.
*Author for correspondence: Peter Rådström. Tel: + 46 46 2223412. Fax: +46 46 2224203. e-mail: Peter.Radstrom@tmb.lth.se
This article has been cited by other articles:
![]() |
N. J. Baxter, L. F. Olguin, M. Golicnik, G. Feng, A. M. Hounslow, W. Bermel, G. M. Blackburn, F. Hollfelder, J. P. Waltho, and N. H. Williams A Trojan horse transition state analogue generated by MgF3- formation in an enzyme active site PNAS, October 3, 2006; 103(40): 14732 - 14737. [Abstract] [Full Text] [PDF] |
||||
![]() |
J.-i. Akutsu, Z. Zhang, M. Tsujimura, M. Sasaki, M. Yohda, and Y. Kawarabayasi Characterization of a Thermostable Enzyme with Phosphomannomutase/Phosphoglucomutase Activities from the Hyperthermophilic Archaeon Pyrococcus horikoshii OT3 J. Biochem., August 1, 2005; 138(2): 159 - 166. [Abstract] [Full Text] [PDF] |
||||
![]() |
J. Palmfeldt, M. Paese, B. Hahn-Hagerdal, and E. W. J. van Niel The Pool of ADP and ATP Regulates Anaerobic Product Formation in Resting Cells of Lactococcus lactis Appl. Envir. Microbiol., September 1, 2004; 70(9): 5477 - 5484. [Abstract] [Full Text] [PDF] |
||||
![]() |
I. C. Boels, M. Kleerebezem, and W. M. de Vos Engineering of Carbon Distribution between Glycolysis and Sugar Nucleotide Biosynthesis in Lactococcus lactis Appl. Envir. Microbiol., February 1, 2003; 69(2): 1129 - 1135. [Abstract] [Full Text] [PDF] |
||||
![]() |
U. Andersson, F. Levander, and P. Radstrom Trehalose-6-phosphate Phosphorylase Is Part of a Novel Metabolic Pathway for Trehalose Utilization in Lactococcus lactis J. Biol. Chem., November 9, 2001; 276(46): 42707 - 42713. [Abstract] [Full Text] [PDF] |
||||
![]() |
J. A. Wouters, H. Frenkiel, W. M. de Vos, O. P. Kuipers, and T. Abee Cold Shock Proteins of Lactococcus lactis MG1363 Are Involved in Cryoprotection and in the Production of Cold-Induced Proteins Appl. Envir. Microbiol., November 1, 2001; 67(11): 5171 - 5178. [Abstract] [Full Text] |
||||
![]() |
F. Levander, U. Andersson, and P. Radstrom Physiological Role of {beta}-Phosphoglucomutase in Lactococcus lactis Appl. Envir. Microbiol., October 1, 2001; 67(10): 4546 - 4553. [Abstract] [Full Text] |
||||
![]() |
U. Nilsson and P. Radstrom Genetic localization and regulation of the maltose phosphorylase gene, malP, in Lactococcus lactis Microbiology, June 1, 2001; 147(6): 1565 - 1573. [Abstract] [Full Text] [PDF] |
||||
![]() |
J. A. Wouters, H. H. Kamphuis, J. Hugenholtz, O. P. Kuipers, W. M. de Vos, and T. Abee Changes in Glycolytic Activity of Lactococcus lactis Induced by Low Temperature Appl. Envir. Microbiol., September 1, 2000; 66(9): 3686 - 3691. [Abstract] [Full Text] |
||||
![]() |
H. Shimizu, T. Mizuguchi, E. Tanaka, and S. Shioya Nisin Production by a Mixed-Culture System Consisting of Lactococcus lactis and Kluyveromyces marxianus Appl. Envir. Microbiol., July 1, 1999; 65(7): 3134 - 3141. [Abstract] [Full Text] |
||||
![]() |
D. Nilsson and M. Kilstrup Cloning and Expression of the Lactococcus lactis purDEK Genes, Required for Growth in Milk Appl. Envir. Microbiol., November 1, 1998; 64(11): 4321 - 4327. [Abstract] [Full Text] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| INT J SYST EVOL MICROBIOL | MICROBIOLOGY | J GEN VIROL |
| J MED MICROBIOL | ALL SGM JOURNALS | |