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Nigella sativa L. seed lipase isolated from defatted seeds was partially purified and used as catalyst in transesterification reactions. Purification of an ammonium sulfate‐precipitated sample (at 35% saturation, Nigella PL ) by DEAE ion‐exchange chromatography increased the specific activity from 13.9 to 156.7 U/mg protein. Nigella PL and Nigella CPL (the partially purified enzyme sample obtained by DEAE ion‐exchange chromatography) catalyzed the transesterification of vinyl acetate with octanol, with racemic sulcatol (6‐methyl‐5‐hepten‐2‐ol), and with racemic trans ‐sobrerol ( trans‐p ‐menth‐6‐ene‐2,8‐diol) in different organic solvents. Both activity and enantioselectivity of the enzyme samples used for these biotransformations were affected by the nature of the organic solvent.
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Tüter et al. (2003) studied this question.
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