The complete utilization of raffinose and melibiose by Saccharomyces cerevisiae requires the synthesis and secretion of an α-galactosidase encoded by a single MEL1 gene. The influence of culture conditions on the productivity of α-galactosidase in batch growth of yeast cells has been investigated. A modulation of the MEL1 gene expression has been observed depending on growth condition, with a maximum of enzyme productivity during a transient physiological phase corresponding to the early stationary phase. Our experiments demonstrate that the highest α-galactosidase productivity observed in the early stationary phase of growth is not associated with a starvation condition, but it is coupled to a particular growth phase. The increase of specific activity of the enzyme occurs mainly for periplasmic and intracellular fractions while the amount of enzyme secreted in the medium remains fairly constant. © 1989.
Porro, D., Martegani, E., Ranzi, B. (1989). GROWTH-PHASE MODULATION OF THE PRODUCTIVITY OF ALPHA-GALACTOSIDASE IN BUDDING YEAST CULTURES. JOURNAL OF BIOTECHNOLOGY, 12(1), 71-78 [10.1016/0168-1656(89)90130-2].
GROWTH-PHASE MODULATION OF THE PRODUCTIVITY OF ALPHA-GALACTOSIDASE IN BUDDING YEAST CULTURES
PORRO, DANILO;MARTEGANI, ENZO;
1989
Abstract
The complete utilization of raffinose and melibiose by Saccharomyces cerevisiae requires the synthesis and secretion of an α-galactosidase encoded by a single MEL1 gene. The influence of culture conditions on the productivity of α-galactosidase in batch growth of yeast cells has been investigated. A modulation of the MEL1 gene expression has been observed depending on growth condition, with a maximum of enzyme productivity during a transient physiological phase corresponding to the early stationary phase. Our experiments demonstrate that the highest α-galactosidase productivity observed in the early stationary phase of growth is not associated with a starvation condition, but it is coupled to a particular growth phase. The increase of specific activity of the enzyme occurs mainly for periplasmic and intracellular fractions while the amount of enzyme secreted in the medium remains fairly constant. © 1989.
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
