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Appl Environ Microbiol. 1993 December; 59(12): 4004-4009
Copyright © 1993, American Society for Microbiology. All Rights Reserved.

Lipase and Esterase Activities of Propionibacterium freudenreichii subsp. freudenreichii

C. Dupuis, C. Corre and P. Boyaval*

Laboratoire de Recherches de Technologie Laitière, 65 Rue de Saint-Brieuc, 35042 Rennes Cédex, France

ABSTRACT

The lipase and esterase activities of eight strains of dairy Propionibacterium freudenreichii subsp. freudenreichii were studied. A lipase activity was detected on whole cells and in the culture supernatant. The highest activity was expressed at 45°C and pH 6.8. An esterase activity was also detected in the culture medium. The electrophoresis of the intracellular fractions of the cells revealed from three to six different esterase activities. Two esterases were common to all the strains. The substrate specificity was dependent on each esterase, but no activity was revealed, in our experimental conditions, on ester substrates with a chain length longer than that of butyrate.


FOOTNOTES

* Corresponding author.


Appl Environ Microbiol. 1993 December; 59(12): 4004-4009
Copyright © 1993, American Society for Microbiology. All Rights Reserved.




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Copyright © 1993 by the American Society for Microbiology. All rights reserved.