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Applied and Environmental Microbiology, November 2005, p. 6651-6656, Vol. 71, No. 11
0099-2240/05/$08.00+0     doi:10.1128/AEM.71.11.6651-6656.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Insights into Actinobacillus succinogenes Fermentative Metabolism in a Chemically Defined Growth Medium

James B. McKinlay,1 J. Gregory Zeikus,1,2 and Claire Vieille2*

Department of Microbiology and Molecular Genetics,1 Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan 488242

Received 17 December 2004/ Accepted 12 June 2005

Chemically defined media allow for a variety of metabolic studies that are not possible with undefined media. A defined medium, AM3, was created to expand the experimental opportunities for investigating the fermentative metabolism of succinate-producing Actinobacillus succinogenes. AM3 is a phosphate-buffered medium containing vitamins, minerals, NH4Cl as the main nitrogen source, and glutamate, cysteine, and methionine as required amino acids. A. succinogenes growth trends and end product distributions in AM3 and rich medium fermentations were compared. The effects of NaHCO3 concentration in AM3 on end product distribution, growth rate, and metabolic rates were also examined. The A. succinogenes growth rate was 1.3 to 1.4 times higher at an NaHCO3 concentration of 25 mM than at any other NaHCO3 concentration, likely because both energy-producing metabolic branches (i.e., the succinate-producing branch and the formate-, acetate-, and ethanol-producing branch) were functioning at relatively high rates in the presence of 25 mM bicarbonate. To improve the accuracy of the A. succinogenes metabolic map, the reasons for A. succinogenes glutamate auxotrophy were examined by enzyme assays and by testing the ability of glutamate precursors to support growth. Enzyme activities were detected for glutamate synthesis that required glutamine or {alpha}-ketoglutarate. The inability to synthesize {alpha}-ketoglutarate from glucose indicates that at least two tricarboxylic acid cycle-associated enzyme activities are absent in A. succinogenes.

* Corresponding author. Mailing address: Department of Biochemistry and Molecular Biology, Michigan State University, 410 Biochemistry Building, East Lansing, MI 48824. Phone: (517) 353-4674. Fax: (517) 353-9334. E-mail: vieille{at}msu.edu.

Applied and Environmental Microbiology, November 2005, p. 6651-6656, Vol. 71, No. 11
0099-2240/05/$08.00+0     doi:10.1128/AEM.71.11.6651-6656.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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