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Degradation of tetrahydrofurfuryl alcohol by Ralstonia eutropha is initiated by an inducible pyrroloquinoline quinone-dependent alcohol dehydrogenase

Article Abstract:

A research was conducted to investigate the growth of the Ralstonia eutropha strain on tetrahydrofurfuryl alcohol (THFA). The degradation of THFA resulted from an unducible quinohemoprotein alcohol dehydrogenase named tetrahydrofurfuryl alcohol dehydrogenase. Enzyme assays were characterized in a final volume of 1.5 ml at 30 degrees C. The strains were grown in aliquots of mineral salt medium to determine their physiological and biochemical properties. Results showed differences from the breakdown of the analogous aromatic compound furfuryl alcohol by P. putida.

Author: Zarnt, Grit, Schrader, Thomas, Andreesen, Jan R.
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1997
Enzymes, Alcohol, Ethanol, Aromatic compounds

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Temperature-dependent fermentation of D-sorbitol in Escherichia coli O157:H7

Article Abstract:

Research was conducted to investigate the effect of growth temperature on the ability of Escherichia coli O157:H7 to ferment D-sorbitol. O157:H7 strains were observed to have a temperature-sensitive sorbitol phenotype. The dehydrogenase activity was inducible by D-sorbitol but not by D-mannitol and was stable at a high temperature. Results indicate that nonsorbitol-fermenting O157:H7 strains express a temperature-sensitive D-sorbitol phenotype.

Author: Grimont, P.A.D., Bouvet, O.M.M., Pernoud, S.
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1999
Genetic aspects, Escherichia coli, Fermentation, Microorganisms, Sorbitol, Temperature effects

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Engineering of the pyruvate dehydrogenase bypass in Saccharomyces cerevisiae: role of the cytosolic Mg(super 2+) and mitochondrial K+ acetaldehyde dehydrogenases Ald6p and Ald4p in acetate formation during alcoholic fermentation

Article Abstract:

The production of acetate by Saccharomyces cerevisiae during alcoholic fermentation was studied by altering amounts of pyruvate decarboxylase, acetaldehyde dehydrogenase, and acetoacetyl coenzyme A synthetase. Only disruptions in acetaldehyde dehydrogenase affected acetate yield.

Author: Remize, Fabienne, Andrieu, Emilie, Dequin, Sylvie
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2000
Microbiology, Saccharomyces, Brewing

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Subjects list: Research, Dehydrogenases, Oxidoreductases
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