Open AccessPurification and characterization of an erythromycin esterase from an erythromycin‐resistant Pseudomonas sp.
Author(s) -
Kim YongHak,
Cha ChangJun,
Cerniglia Carl E.
Publication year - 2002
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.1574-6968.2002.tb11187.x
Subject(s) - erythromycin , oleandomycin , esterase , chemistry , enzyme , pseudomonas , substrate (aquarium) , biochemistry , lipase , chromatography , stereochemistry , antibiotics , biology , bacteria , ecology , genetics
An erythromycin esterase (molecular mass 51 200 Da) was purified from Pseudomonas sp. GD100, which was isolated from a salmon hatchery sediment sample from Washington State. The p I of the protein was 4.5–4.8. The enzyme was inhibited by 1 mM mercuric acid, and had the substrate specificity for structurally related 14‐membered macrolides, which decreased in the order of oleandomycin, erythromycin A and erythromycin A enol ether. The activity for erythromycin A varied with temperature, but the effect of pH was minimal at pH 6.0–9.0. The half‐life of the enzyme was estimated to be 8.9 h at 35°C and 0.23 h at 55°C, and the activation energy of the catalytic reaction of erythromycin A was estimated at 16.2 kJ mol −1 .