Purification and Characterization of lipase from B.subtilis Pa2

ABSTRACT The extracellular lipase produced by B.subtilis Pa2 was purified by acetone precipitation and Ion exchange chromatography. The molecular weight of the pure protein was estimated to be 19.4 &19.2 kDa by SDS-PAGE. The lipase formed high molecular weight aggregates with molecular weight more than 100,000 kDa. The enzyme was most active in the pH range of 7 to 9 with maximum activity at pH 8, whereas it was most stable in the pH range 5 to 10, retaining more than 70% activity.The present lipase was most active in temperature between 30 and 50 °C.  Mg2+ was found to stimulate lipase activity.