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.