Articles in Press
Volume 2 Issue 1
Molecular Cloning, Overexpression, Purification, Immobilization and Characterization
of Lipase from Staphylococcus pasteuri
Magdy M Yousef, H Elsawy*
Thermostable lipase from Staphylococcus pasteuri was cloned, purified, immobilized and characterized. In this study, lipase gene was expressed in Escherichia coli and purified by DEAE-Sepharose and Glutathione S-sepharose 4B gel column chromatography. Lipase enzyme was purified to homogeneity by 28 times with a final yield of 175 %. The molecular weight of the purified enzyme was estimated to be 53 kDa on SDS-PAGE. The enzyme was successfully immobilized in calcium alginate gelatin composites in the presence of glutaraldehyde.