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J Bacteriol. 1968 August; 96(2): 479-486
Copyright © 1968 American Society for Microbiology. All Rights Reserved.

Enzyme Pattern and Aerobic Growth of Saccharomyces cerevisiae Under Various Degrees of Glucose Limitation

Christoph Beck1 and H. Kaspar Von Meyenburg

a Institute of Microbiology, Federal Institute of Technology, 8006 Zürich, Switzerland

ABSTRACT

The enzyme pattern of Saccharomyces cerevisiae was followed during batch growth and in continuous culture in a synthetic medium limited for glucose under aerobic conditions. Seven enzymes were measured: succinate-cytochrome c oxidoreductase, malate dehydrogenase, nicotinamide adenine dinucleotide-linked glutamate dehydrogenase, malate synthase, isocitrate lyase, aldolase, and nicotinamide adenine dinucleotide phosphate (NADP+)-linked glutamate dehydrogenase. During fermentation of glucose and high growth rate (µ) during the first log phase in batch experiments, the first five enzymes (group I) were repressed, and aldolase and NADP+-linked glutamate dehydrogenase (group II) were derepressed. During growth on the accumulated ethyl alcohol and lower µ, the group I enzymes were preferentially formed and the other two were repressed. A sequence of derepression of the group I enzymes was found during the shift from glucose to ethyl alcohol metabolism, which can be correlated with a strong increase in the percentage of single (nonbudding) cells in the population. A correlation between the state of cells in the budding cycle and enzyme repression and derepression is suggested. In continuous culture, the enzyme pattern was shown to be related to the growth rate. The group I enzymes were repressed at high growth rates, while the group II enzymes were derepressed. Each enzyme exhibits a different dependence. The enzyme pattern is shown to depend on the rate of substrate consumption as well as on the type of metabolism and to be correlated with the budding cycle. The enzyme pattern is considered to be controlled by changes of intracellular catabolic or metabolic conditions inherent in the division cycle.


FOOTNOTES

1 Present address: Department of Bacteriology, University of California, Davis, Calif. 95616.


J Bacteriol. 1968 August; 96(2): 479-486
Copyright © 1968 American Society for Microbiology. All Rights Reserved.




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