상세 정보

underline
Metadata Downloads : dc(xml) or Excel
Cited 0 time in scopus ci

Title 

Occurrence of ofloxacin ester-hydrolyzing esterase from Bacillus niacini EM001

Authors 

H K KimH S NaM S ParkTae Kwang OhT S Lee

Publisher 

Elsevier

Issue Date 

2004

Citation 

Journal of Molecular Catalysis B:Enzymatic, vol. 27, no. 4, pp. 237-241

Keywords 

bacillus niaciniesteraselevofloxacinofloxacinestersester derivativebacillusbacillus subtilis

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%.

ISSN 

1381-1177

Link 

http://dx.doi.org/10.1016/j.molcatb.2003.11.007

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


There are no files associated with this item.
qrcode

FusionCharts.
DSpace Software Coptright(c) 2010 MIT and Hewleft-Packard  /  KRIBB-REPOSITORY ( Email:jakim@kribb.re.kr)