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Isolation and characterization of carboxylesterase E 3 from Salmonella enteriea
Author(s) -
Brisabois Anne,
Goullet P.
Publication year - 1993
Publication title -
journal of applied bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.889
H-Index - 156
eISSN - 1365-2672
pISSN - 0021-8847
DOI - 10.1111/j.1365-2672.1993.tb02764.x
Subject(s) - carboxylesterase , biology , salmonella , esterase , escherichia coli , phylogenetic tree , enterobacteriaceae , microbiology and biotechnology , serotype , gene , salmonella enterica , enzyme , biochemistry , genetics , bacteria
Three esterases (Est‐) hydrolysing α‐naphthyl acetate: Est‐E 1 , Est‐E 3 and Est‐E 4 produced by Salmonella enterica serovar Typhimurium, strain LT2 were separated by DEAE chromatography and gel filtration. Est‐E 3 , the major component of this set of enzymes, clearly differed from the two other esterases by its apparent molecular weight, titration curve, substrate specificity and inactivation. Immunoglobulins raised against Est‐E 3 completely neutralized the activity of Est‐E 3 but did not react with Est‐E 1 or Est‐E 4 ; it showed no cross reaction with carboxylesterase B of Escherichia coli or with carboxylesterases from other enterobacteria. Est‐E 3 showed electrophoretic variants which were biochemically and immunologically detected in the seven subspecies of the genus Salmonella . These findings suggest that variants of Est‐E 3 are the products of very closely related loci originating from a common ancestral gene. The esterase could be a phylogenetic marker of the genus and a suitable molecular tool for taxonomy and epidemiology.