Title of article :
Purification and properties of lipase from a Bacillus strain for catalytic resolution of (R)-Naproxen
Author/Authors :
Zhang، نويسنده , , Jinhong and Hou، نويسنده , , Zhibo and Yao، نويسنده , , Chuanyi and Yu، نويسنده , , Yaoting، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2002
Pages :
6
From page :
205
To page :
210
Abstract :
A Bacillus strain was screened for asymmetric resolution of (R)-Naproxen. The optical purity (ee (%)) of (R)-Naproxen was found to be 86.47% and conversion rate was 40–50% in bacterial cells PBS reaction system. The dissolved lipase was clarified from the Bacillus bacterial cells by centrifugation and loaded on a phenyl-Sepharose CL-4B column. After purification by a single hydrophobic chromatography, the activity of lipase was approximately 43 times higher than the crude one. The hydrolytic activity of lipase using Naproxen ethyl ester and p-nitrophenyl acetate (p-NPA) as substrate remained essentially constant during the purification procedure. A Bacillus strain with stereochemical selectivity was obtained.
Keywords :
Asymmetric resolution , Lipase , Purification , (R)-Naproxen , hydrophobic chromatography
Journal title :
Journal of Molecular Catalysis B Enzymatic
Serial Year :
2002
Journal title :
Journal of Molecular Catalysis B Enzymatic
Record number :
1709370
Link To Document :
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