期刊
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
卷 27, 期 4-6, 页码 237-241出版社
ELSEVIER
DOI: 10.1016/j.molcatb.2003.11.007
关键词
esterase; Bacillus niacini; levofloxacin; ofloxacin
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 (M-r) of 54,098 kDa. Based on the M-r 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 degreesC 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 ee(p) of 67% until the conversion rate become up to 35%. (C) 2003 Elsevier B.V. All rights reserved.
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