Involvement of pyruvate oxidase activity and acetate production in the survival of Lactobacillus plantarum during the stationary phase of aerobic growth

Applied and Environmental Microbiology

Volumn 72, Issue 12, 2006, Pages 7933-7940

  Goffin, Philippe ^a,c   Muscariello, Lidia ^b   Lorquet, Frederique ^a,d   Stukkens, Aline ^a   Prozzi, Deborah ^a   Sacco, Margherita ^b   Kleerebezem, Michiel ^c   Hols, Pascal ^a  

^a UNIVERSITÉ CATHOLIQUE DE LOUVAIN   (Belgium)

^b SECOND UNIVERSITY OF NAPLES   (Italy)

^c NIZO FOOD RESEARCH   (Netherlands)

^d CEMAGREF   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYMES; FERMENTATION; GENES; GLUCOSE; GROWTH KINETICS; POTASSIUM COMPOUNDS;

AEROBIC GROWTH; LACTOBACILLUS PLANTARUM; MALTOSE FERMENTATION; PYRUVATE OXIDASE;

BACTERIA;

ACETIC ACID; CARBON; GLUCOSE; LACTIC ACID; MALTOSE; POXB PROTEIN; POXC PROTEIN; POXD PROTEIN; POXE PROTEIN; POXF PROTEIN; PYRUVATE OXIDASE;

ACETATE; BACTERIUM; ENZYME ACTIVITY; FERMENTATION; GROWTH CURVE; METABOLISM; MUTATION; OXIC CONDITIONS; SURVIVAL;

AEROBIC METABOLISM; ARTICLE; BACTERIAL GENE; BACTERIAL GENOME; BACTERIAL GROWTH; BACTERIAL SURVIVAL; BACTERIUM MUTANT; BIOSYNTHESIS; CATABOLITE REPRESSION; CONTROLLED STUDY; ENZYME ACTIVITY; FERMENTATION; GENE INACTIVATION; KNOCKOUT GENE; LACTOBACILLUS PLANTARUM; NONHUMAN; NUCLEOTIDE SEQUENCE; POXB GENE; POXC GENE; POXD GENE; POXE GENE; POXF GENE;

ACETATES; AEROBIOSIS; BACTERIAL PROTEINS; BASE SEQUENCE; BIOTECHNOLOGY; GENE EXPRESSION REGULATION, BACTERIAL; LACTOBACILLUS PLANTARUM; MOLECULAR SEQUENCE DATA; MUTATION; PYRUVATE OXIDASE;

LACTOBACILLUS PLANTARUM;

EID: 33845520090     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.00659-06     Document Type: Article

References (31)

1. Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
2. Condon, S. 1987. Responses of lactic-acid bacteria to oxygen. FEMS Microbiol. Rev. 46:269-280.
3. Dirar, H., and E. B. Collins. 1973. Aerobic utilization of low concentrations of galactose by Lactobacillus plantarum. J. Gen. Microbiol. 78:211-215.
4. Gilliland, S. E. 1985. Bacterial starters cultures in food. CRC Press, Inc., Boca Raton, Fla.
5. Gobbetti, M., P. Lavermicocca, F. Minervini, M. De Angelis, and A. Corsetti. 2000. Arabinose fermentation by Lactobacillus plantarum in sourdough with added pentosans and α-L-arabinofuranosidase: a tool to increase the production of acetic acid. J. Appl. Microbiol. 88:317-324.
6. Goffin, P., F. Lorquet, M. Kleerebezem, and P. Hols. 2004. Major role of NAD-dependent lactate dehydrogenases in aerobic lactate utilization in Lactobacillus plantarum during early stationary phase. J. Bacteriol. 186:6661-6666.
7. Hols, P., C. Defrenne, T. Ferain, S. Derzelle, B. Delplace, and J. Delcour. 1997. The alanine racemase gene is essential for growth of Lactobacillus plantarum. J. Bacteriol. 179:3804-3807.
8. Josson, K., T. Scheirlinck, F. Michiels, C. Platteeuw, P. Stanssens, H. Joos, P. Dhaese, M. Zabeau, and J. Manillon. 1989. Characterization of a gram-positive broad-host-range plasmid isolated from Lactobacillus hilgardii. Plasmid 21:9-20.
9. Kleerebezem, M., J. Boekhorst, R. van Kranenburg, D. Molenaar, O. P. Kuipers, R. Leer, R. Tarchini, S. A. Peters, H. M. Sandbrink, M. W. Fiers, W. Stiekema, R. M. Lankhorst, P. A. Bron, S. M. Hoffer, M. N. Groot, R. Kerkhoven, M. de Vries, B. Ursing, W. M. de Vos, and R. J. Siezen. 2003. Complete genome sequence of Lactobacillus plantarum WCFS1. Proc. Natl. Acad. Sci. USA 100:1990-1995.
10. Liu, S. Q., R. Holland, and V. L. Crow. 2003. The potential of dairy lactic acid bacteria to metabolize amino acids via non-transaminating reactions and endogenous transamination. Int. J. Food Microbiol. 86:257-269.
11. Liu, S. Q., R. Holland, P. McJarrow, and V. L. Crow. 2003. Serine metabolism in Lactobacillus plantarum. Int. J. Food Microbiol. 89:265-273.
12. Lorquet, F., P. Goffin, L. Muscariello, J. B. Baudry, V. Ladero, M. Sacco, M. Kleerebezem, and P. Hols. 2004. Characterization and functional analysis of the poxB gene, which encodes pyruvate oxidase in Lactobacillus plantarum. J. Bacteriol. 186:3749-3759.
13. Miller, R. A., and B. E. Britigan. 1997. Role of oxidants in microbial patho-physiology. Clin. Microbiol. Rev. 10:1-18.
14. Molin, G. 2001. Probiotics in foods not containing milk or milk constituents, with special reference to Lactobacillus plantarum 299v. Am. J. Clin. Nutr. 73:3805-3855.
15. Muller, Y. A., Y. Lindqvist, W. Furey, G. E. Schulz, F. Jordan, and G. Schneider. 1993. A thiamin diphosphate binding fold revealed by comparison of the crystal structures of transketolase, pyruvate oxidase, and pyruvate decarboxylase. Structure 1:95-103.
16. Muller, Y. A., and G. E. Schulz. 1993. Structure of the thiamine- and flavin-dependent enzyme pyruvate oxidase. Science 259:965-967.
17. Muller, Y. A., G. Schumacher, R. Rudolph, and G. E. Schulz. 1994. The refined structures of a stabilized mutant and of wild-type pyruvate oxidase from Lactobacillus plantarum. J. Mol. Biol. 237:315-335.
18. Murphy, M. G., and S. Condon. 1984. Comparison of aerobic and anaerobic growth of Lactobacillus plantarum in a glucose medium. Arch. Microbiol. 138:49-53.
19. Murphy, M. G., and S. Condon. 1984. Correlation of oxygen utilization and hydrogen peroxide accumulation with oxygen induced enzymes in Lactobacillus plantarum cultures. Arch. Microbiol. 138:44-48.
20. Murphy, M. G., L. O'Connor, D. Walsh, and S. Condon. 1985. Oxygen-dependent lactate utilization by Lactobacillus plantarum. Arch. Microbiol. 141:75-79.
21. Muscariello, L., R. Marasco, M. De Felice, and M. Sacco. 2001. The functional ccpA gene is required for carbon catabolite repression in Lactobacillus plantarum. Appl. Environ. Microbiol. 67:2903-2907.
22. Patton, T. G., K. C. Rice, M. K. Foster, and K. W. Bayles. 2005. The Staphylococcus aureus cidC gene encodes a pyruvate oxidase that affects acetate metabolism and cell death in stationary phase. Mol. Microbiol. 56:1664-1674.
23. Pericone, C. D., S. Park, J. A. Imlay, and J. N. Weiser. 2003. Factors contributing to hydrogen peroxide resistance in Streptococcus pneumoniae include pyruvate oxidase (SpxB) and avoidance of the toxic effects of the Fenton reaction. J. Bacteriol. 185:6815-6825.
24. Risse, B., G. Stempfer, R. Rudolph, H. Mollering, and R. Jaenicke. 1992. Stability and reconstitution of pyruvate oxidase from Lactobacillus plantarum: dissection of the stabilizing effects of coenzyme binding and subunit interaction. Protein Sci. 1:1699-1709.
25. Russell, P., L. P. Hager, and R. B. Gennis. 1977. Characterization of the proteolytic activation of pyruvate oxidase. Control by specific ligands and by the flavin oxidation-reduction state. J. Biol. Chem. 252:7877-7882.
26. Sambrook, J., E. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory Press, New York, N.Y.
27. Sedewitz, B., K. H. Schleifer, and F. Gotz. 1984. Physiological role of pyruvate oxidase in the aerobic metabolism of Lactobacillus plantarum. J. Bacteriol. 160:462-465.
28. Sedewitz, B., K. H. Schleifer, and F. Gotz. 1984. Purification and biochemical characterization of pyruvate oxidase from Lactobacillus plantarum. J. Bacteriol. 160:273-278.
29. Shah, N. P. 2000. Probiotic bacteria: selective enumeration and survival in dairy foods. J. Dairy Sci. 83:894-907.
30. van Kranenburg, R., J. D. Marugg, I.I. van Swam, N. J. Willem, and W. M. de Vos. 1997. Molecular characterization of the plasmid-encoded eps gene cluster essential for exopolysaccharide biosynthesis in Lactococcus lactis. Mol. Microbiol. 24:387-397.
31. Wille, G., M. Ritter, M. S. Weiss, S. Konig, W. Mantele, and G. Hubner. 2005. The role of Val-265 for flavin adenine dinucleotide (FAD) binding in pyruvate oxidase: FTIR, kinetic, and crystallographic studies on the enzyme variant V265A. Biochemistry 44:5086-5094.