Purification and characterization of lipase from wheat (Triticum aestivum L.) germ

A method of isolation and purification of lipase (EC 3.1.1.3) from the germ of wheat (Triticum aestivum L.) is described. An electrophoretically homogeneous preparation of the enzyme (specific activity, 622.5 x 10(-3) mumol/min per mg protein) was obtained after 61-fold purification. The molecular weight of the enzyme, determined by gel chromatography, was 143 +/- 2 kDa. The optimal conditions for the enzyme were 37degreesC and pH 8.0. The homogeneous preparation of the lipase exhibited high thermal stability: over 20% of the original activity was retained after incubation of the preparation at high temperatures (60-90degreesC) for 1 h at pH 8.0.