Is Escherichia coli growing in glucose-limited chemostat culture able to utilize other sugars without lag?
Article Abstract:
A study of the ability of glucose-restricted chemostat culture-grown Escherichia coli to utilize a group of other sugars without any lag time reveals that mannose, fructose, ribose and maltose are utilized for growth immediately by cells that grow at 0.2, 0.3 and 0.6 per hour dilution rates, while growth with galactose is delayed despite its immediate transport. Arabinose is not transported or consumed for growth, indicating that chemostat-grown E. coli cells have the potential to utilize sugars other than glucose as an alternate source of carbon and energy, without any lag period.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1995
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A reassessment of the genetic determinants, the effect of growth conditions and the availability of an electron donor on the nitrosating activity of Escherichia coli K-12
Article Abstract:
Research shows that the bacteria Escherichia coli K-12 expresses high nitrosation activity in anaerobic conditions and minimal nutrients glycerol and fumarate. Experiments using mutant strains of E. coli incapable of anaerobic induction in electron transfer chains demonstrate that the respiratory nitrate reductase encoded by the narGHJI operon is active in nitrosation. Over 400 independent cultures of E. coli K-12 were analysed to ascertain genetic determinants.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1997
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Suppression of Escherichia coli formate hydrogenlyase activity by trimethylamine N-oxide is due to drainage of the inducer formate
Article Abstract:
Research shows that formate hydrogenlyase H(FDH-H) enzyme activity in Escherichia coli bacteria is not expressed in the presence of 40 millimoles trimethylamine N-oxide (TMAO). Evidence indicates that less formate is available for the formate hydrogenlyase pathway in the presence of formate-dependent reduction of TMAO via anaerobic enzymes FDH-N and TMAO reductase activity.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1997
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