Dynamics and regulation of sucrose phosphorylase formation in Leuconostoc mesenteroides fermentations
Article first published online: 18 FEB 2004
Copyright © 1987 John Wiley & Sons, Inc.
Biotechnology and Bioengineering
Volume 29, Issue 1, pages 8–15, January 1987
How to Cite
Vandamme, E. J., Van Loo, J. and De Laporte, A. (1987), Dynamics and regulation of sucrose phosphorylase formation in Leuconostoc mesenteroides fermentations. Biotechnol. Bioeng., 29: 8–15. doi: 10.1002/bit.260290103
- Issue published online: 18 FEB 2004
- Article first published online: 18 FEB 2004
- Manuscript Accepted: 31 DEC 1985
The production of Leuconostoc mesenteroides sucrose phosphorylase has been studied in 10- and 20-L batch fermentations. A fermentation medium was devised combining rapid growth, high cell yield, and high enzyme levels. Overall fermentation dynamics and enzyme fermentation patterns are elucidated here in detail. Sucrose is phosphorolyzed into fructose and glucose-1-phosphate (G-1-P) with G-1-P preferentially utilized (thus saving ATP). Subsequently, fructose is gradually metabolized and is also converted to mannitol. Invertase activity is absent. Sucrose phosphorylase is formed transitorily with peak levels toward the end of active growth; a sharp decline in enzyme activity occurs upon further fermentation. The moment of cell (enzyme) harvest is thus critical in view of obtaining active cell or enzyme preparations for sucrose phosphorolysis. Microaerophilic and strictly anaerobic fermentations displayed no appreciable difference in sucrose phosphorylase formation profile. The enzyme is intracellularly located. It is constitutively formed in the absence of sucrose, contrary to that of Pseudomonas species; other disaccharide phosphorylases are not formed.