Abstract
A method of isolation and purification of lipase (EC 3.1.1.3) from the germ of wheat (Triticum aestivumL.) is described. An electrophoretically homogeneous preparation of the enzyme (specific activity, 622.5 × 10–3 μmol/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 37°C 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 (60–90°C) for 1 h at pH 8.0.
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Kapranchikov, V.S., Zherebtsov, N.A. & Popova, T.N. Purification and Characterization of Lipase from Wheat (Triticum aestivum L.) Germ. Applied Biochemistry and Microbiology 40, 84–88 (2004). https://doi.org/10.1023/B:ABIM.0000010360.46824.56
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DOI: https://doi.org/10.1023/B:ABIM.0000010360.46824.56