Purification and application of a lipase from Penicillium expansum PED-03.
An extracellular lipase was purified from the fermentation broth of Penicillium expansum PED-03 by DEAE-Sepharose chromatography, followed by sephacryl S-200 chromatography. The enzyme was purified 81.8-fold with 19.8% recovery and a specific activity of 85.94 U/mg. The molecular weight of the homogeneous enzyme was about 28 kDa, determined by sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis. The enzymatic resolution of racemic ibuprofen was carried out by the lipase from P. expansum PED-03, and the conversion reached 46% with excellent enantioselectivity(E > 200), which showed a good application potential in the production of optically pure ibuprofen.
Lianghua
Tang
T
Department of Chemical Engineering and Bioengineering, Zhejiang University, Hangzhou, 310027, China. biotlh@fjnu.edu.cn
Liming
Xia
X
Min
Su
S
Huaying
Guo
G
D004795:Enzyme Stability; D007052:Ibuprofen / Q000737:chemistry; D007218:Industrial Microbiology; D007536:Isomerism; D008049:Lipase / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification*; D010407:Penicillium / Q000201:enzymology*
D008049:Lipase; D007052:Ibuprofen