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Applied and Environmental Microbiology, December 2007, p. 7732-7739, Vol. 73, No. 23
0099-2240/07/$08.00+0     doi:10.1128/AEM.01260-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Growth Characteristics of Brevibacterium, Corynebacterium, Microbacterium, and Staphylococcus spp. Isolated from Surface-Ripened Cheese{triangledown}

Jérôme Mounier,1,2,{dagger} Mary C. Rea,2 Paula M. O'Connor,1 Gerald F. Fitzgerald,2 and Timothy M. Cogan1,2*

Moorepark Food Research Centre, Fermoy, County Cork, Ireland,1 Department of Microbiology, University College, Cork, Ireland2

Received 7 June 2007/ Accepted 26 September 2007

The growth characteristics of five bacteria, Brevibacterium aurantiacum 1-16-58, Corynebacterium casei DPC 5298T, Corynebacterium variabile DPC 5310, Microbacterium gubbeenense DPC 5286T, and Staphylococcus saprophyticus 4E61, all of which were isolated from the surface of smear cheese, were studied in complex and chemically defined media. All of the coryneforms, except M. gubbeenense, grew in 12% salt, while B. aurantiacum and S. saprophyticus grew in 15% salt. All five bacteria assimilated lactate in a semisynthetic medium, and none of the coryneform bacteria assimilated lactose. Glucose assimilation was poor, except by S. saprophyticus and C. casei. Five to seven amino acids were assimilated by the coryneforms and 12 by S. saprophyticus. Glutamate, phenylalanine, and proline were utilized by all five bacteria, whereas utilization of serine, threonine, aspartate, histidine, alanine, arginine, leucine, isoleucine, and glycine depended on the organism. Growth of C. casei restarted after addition of glutamate, proline, serine, and lactate at the end of the exponential phase, indicating that these amino acids and lactate can be used as energy sources. Pantothenic acid was essential for the growth of C. casei and M. gubbeenense. Omission of biotin reduced the growth of B. aurantiacum, C. casei, and M. gubbeenense. All of the bacteria contained lactate dehydrogenase activity (with both pyruvate and lactate as substrates) and glutamate pyruvate transaminase activity but not urease activity.

* Corresponding author. Mailing address: Moorepark Food Research Centre, Teagasc, Moorepark, Fermoy, Co. Cork, Ireland. Phone: 353 25 42227. Fax: 353 25 42340. E-mail: tim.cogan{at}teagasc.ie

{triangledown} Published ahead of print on 5 October 2007.

{dagger} Present address: UMR GMPA, INRA, 78850 Thiverval-Grignon, France.

Applied and Environmental Microbiology, December 2007, p. 7732-7739, Vol. 73, No. 23
0099-2240/07/$08.00+0     doi:10.1128/AEM.01260-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.





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