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. 1995 Apr;61(4):1661–1665. doi: 10.1128/aem.61.4.1661-1665.1995

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

P Gilot 1, P Andre 1
PMCID: PMC167427  PMID: 7747982

Abstract

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.

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Selected References

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