Lipase from Vicia faba minor

Lipase was partially purified from small faba beans by ethanol precipitation and Sephadex gel filtration and characterised by disc gel electrophoresis, isoelectric focusing and molecular weight determination in the presence of sodium dodecyl sulphate. Kinetic studies demonstrated that the properties of the enzyme conformed generally to those of lipases from other sources. The isoelectric point was pH 4·8, and electrophoresis at pH 9·3 revealed one lipase band in the R_f0·25–0·31 region. The molecular weight was 210,000 ± 20,000. The possible importance of lipase is discussed with respect to the degradation of small faba bean lipids and to chemical changes occurring during storage of processed faba beans.