Regulation of product formation during glucose or lactose limitation in nongrowing cells of Streptococcus lactis
- 1 August 1984
- journal article
- research article
- Published by American Society for Microbiology in Applied and Environmental Microbiology
- Vol. 48 (2) , 332-337
- https://doi.org/10.1128/aem.48.2.332-337.1984
Abstract
Nongrowing cells of Streptococcus lactis in a pH-stat were dosed with sugar to allow fermentation at the maximum rate or were fed a continuous supply of sugar at rates less than the maximum. Under anaerobic conditions, rapid fermentation of either glucose or lactose was essentially homolactic. However, with strain ML3, limiting the fermentation rate diverted approximately half of the pyruvate to formate, acetate, and ethanol. At limiting glucose fermentation rates, cells contained lower concentrations of lactate dehydrogenase activator (fructose 1,6-diphosphate) and pyruvate formate-lyase inhibitors (triose phosphates). As a result, pyruvate formate-lyase and pyruvate dehydrogenase play a greater role in pyruvate metabolism. In contrast to strain ML3, strain ML8 did not give the same diversion of products under anaerobic conditions, and cells retained higher concentrations of the above effector compounds. Lactose metabolism under aerobic conditions resulted in pyruvate excretion by both S. lactis ML3 and ML8. At 7% of the maximum utilization rate, pyruvate accounted for 69 and 35% of the lactose metabolized by ML3 and ML8, respectively. Acetate was also a major product, especially with ML8. The data suggest that NADH oxidase is involved in coenzyme recycling in the presence of oxygen and that pyruvate formate-lyase is inactivated, but the pyruvate dehydrogenase complex still functions.This publication has 31 references indexed in Scilit:
- Enzymatic measurement of ethanol or NAD in acid extracts of biological samplesAnalytical Biochemistry, 1983
- Lactose Hydrolysing Enzymes inStreptococcus lactisandStreptococcus cremorisand also in some other Species of StreptococciJournal of Applied Bacteriology, 1980
- Determination of acetaldehyde in blood using automated distillation and fluorometryAnalytical Biochemistry, 1978
- Purification and properties of pyruvate kinase from Streptococcus lactisBiochimica et Biophysica Acta (BBA) - Enzymology, 1976
- Tagatose-1,6-diphosphate activation of lactate dehydrogenase from Streptococcus cremorisBiochemical and Biophysical Research Communications, 1975
- Determination of protein: A modification of the lowry method that gives a linear photometric responseAnalytical Biochemistry, 1972
- Molar Growth Yields and Fermentation Balances of Lactobacillus casei L3 in Batch Cultures and in Continuous CulturesJournal of General Microbiology, 1970
- Multiple forms of phosphoenolpyruvate carboxylase from Chlamydomonas reinhardtiiBiochimica et Biophysica Acta (BBA) - Protein Structure, 1970
- An enzymic method for the measurement of inorganic phosphateAnalytical Biochemistry, 1967
- Fructose-1,6-diphosphate Requirement of Streptococcal Lactic DehydrogenasesScience, 1964