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[Purification and characterization of lipases from wheat germ]
V S Kapranchikov1, N A Zherebtsov, T N Popova
1Voronezh State Technological Academy, pr. Revolyutsii 19, Voronezh, 394017 Russia.
Abstract:
A method of isolation and purification of lipase (EC 3.1.1.3) from the germ of wheat (Triticum aestivum) is described. Electrophoretically homogeneous preparation of the enzyme (specific activity, 622.5 x x 10(-3) mumol/min per mg protein) was obtained after purification in 61 times. The molecular weight of the enzyme, determined by gel chromatography, was 143 +/- 2 kDa. The optimal conditions for the enzyme were 37 degrees and pH 8.0. Homogeneous preparation of the lipase exhibited high thermal stability: over 20% of original activity was retained after incubation of the preparation at high temperatures (60-90 degrees) for 1 h at pH 8.0.