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Appl. Environ. Microbiol., Apr 1995, 1661-1665, Vol 61, No. 4
Copyright © 1995, American Society for Microbiology

Characterization of five esterases from Listeria monocytogenes and use of their electrophoretic polymorphism for strain typing

P Gilot and P Andre
Departement de Microbiologie, Institut d'Hygiene et d'Epidemiologie, Brussels, Belgium.

Esterases from Listeria monocytogenes strains isolated from cheeses were analyzed by starch gel electrophoresis. Five esterases, numbered from EST 1 to EST 5 in order of decreasing anodal migration, were identified. The EST 1, EST 3, EST 4, and EST 5 set was most active toward alpha-naphthyl propionate, while EST 2 was most active toward alpha-naphthyl acetate. Results from inhibitor studies suggest that all of these esterases were EC class 3.1.1.1 carboxylesterases, except that EST 1 and EST 3 also showed some sensitivity to parahydroxymercuribenzoate. Polymorphism of these five esterases was observed in the population. Twelve esterase patterns were defined and used to subdivide serotypes.


This article has been cited by other articles:

  • GILOT, P., JOSSIN, Y., CONTENT, J. (2000). Cloning, sequencing and characterisation of a Listeria monocytogenes gene encoding a fibronectin-binding protein. J Med Microbiol 49: 887-896 [Abstract] [Full Text]  
  • Gilot, P., Gubina, M., Klun, N., Mehle, J., Tcherneva, E., Rijpens, N., Herman, L. (1999). Typing of Listeria monocytogenes Strains by Repetitive Element Sequence-Based PCR. J. Clin. Microbiol. 37: 103-109 [Abstract] [Full Text]  


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