Author : Fadhil Redha, Asia
karbala journal of pharmaceutical sciences,
Volume 6, Issue 9, Pages 6-15
Many lipases have been extensively purified and characterized in terms of their activity and
stability profiles relative to pH, temperature, and their effects as metal ions and chelating agents.
One hundred samples were collected from different body sites and lesions of in and out patients
who attented Al-Kadhumiyah and Baghdad Teaching Hospitals. Identification of bacterial
isolates was performed by following the procedures mentioned elsewhere in the literature.
Purification steps of lipase included: extraction of the enzyme, precipitation of the enzyme by
ammonium sulphate, dialysis, ion-exchange chromatography, and gel filtration chromatography.
The results revealed that the enzyme was purified with a yield of 0.3 and a fold of purification of
153.7. Also, the optimum temperature and pH for lipase stability were 40 0C and pH 8,
respectively, while the molecular weight of the enzyme was 110000 daltons.