Occurrence of ofloxacin ester-hydrolyzing esterase from Bacillus niacini EM001

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Title
Occurrence of ofloxacin ester-hydrolyzing esterase from Bacillus niacini EM001
Author(s)
H K Kim; H S Na; M S Park; Tae Kwang Oh; T S Lee
Bibliographic Citation
Journal of Molecular Catalysis B: Enzymatic, vol. 27, no. 4, pp. 237-241
Publication Year
2004
Abstract
A Bacillus niacini strain (EM001) producing an ofloxacin ester-enantioselective esterase was isolated from the soil samples collected near Taejon, Korea. The cloned gene showed that the esterase EM001 composed of 495 amino acids corresponding to a relative molecular weight (Mr) of 54,098kDa. Based on the Mr and the protein sequence, the esterase EM001 was similar to p-nitrobenzyl esterase from Bacillus subtilis with an identity of 41.8%. The optimum temperature and pH of the purified His-tagged enzyme were 45°C and 9.0, respectively. The purified esterase EM001 hydrolyzed preferably (R)-ofloxacin propyl ester than (S)-form ester at the initial reaction phase with an eeP of 67% until the conversion rate become up to 35%.
Keyword
Bacillus niaciniEsteraseLevofloxacinOfloxacin
ISSN
1381-1177
Publisher
Elsevier
DOI
http://dx.doi.org/10.1016/j.molcatb.2003.11.007
Type
Article
Appears in Collections:
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
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