Open AccessPurification and characterization of three carboxylesterases from Enterobacteriaceae
Author(s) -
Goullet Philippe,
Brisabois Anne,
Picard Bertrand
Publication year - 1993
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1993.tb06077.x
Subject(s) - citrobacter , proteus vulgaris , enterobacteriaceae , enzyme , salmonella enterica , proteus , isopropyl , salmonella , diisopropyl fluorophosphate , chemistry , microbiology and biotechnology , biochemistry , bacteria , hydrolysis , biology , chromatography , escherichia coli , organic chemistry , gene , genetics
The carboxylesterases from Proteus vulgaris, Salmonella enterica and Citrobacter amalonaticus were purified 104‐, 95‐ and 120‐fold, respectively by chromatography. The enzymes had similar catalytic activities but differed considerably in their inactivation by heat, di‐isopropyl fluorophosphate and Cd 2+ , Zn 2+ , Hg 2+ and Cu 2+ . Quantitative neutralization of hydrolytic activity with specific immunoglobulins indicated that the three enzymes were antigenically distinct.