Abstract
AbstractSelective hydrolysis of borage (Borago officinalis L.) oil was catalyzed by two lipase preparations of Nigella sativa L. seeds at 40°C in a mixture of borage oil, water, and hexane. Ammonium sulfate‐precipitated lipase (Nigella PL) and lipase partially purified by DEAE‐ion exchange chromatography (Nigella CPL) exhibited a negative specificity toward γ‐linolenic acid (GLA). Best results were obtained in the experiments conducted with 330 U/g oil of Nigella PL and 200 U/g oil of nigella CPL. When 330 U/g oil of Nigella PL was used, after 8 h the GLA level rose from 21.9% in the starting oil to 29.6 and 41.8% in TAG and DAG fractions of the product mixtures, respectively (1.5‐fold enrichment of GLA in the total unhydrolyzed acylglycerol fraction). At 200 U/g oil enzyme concentration of Nigella CPL, after 77 h maximum GLA enrichment was observed in the DAG fraction. The GLA content of the DAG increased to 34.6%, corresponding to almost 1.6‐fold enrichment. The relative inability of Nigella sativa lipase(s) to hydrolyze γ‐linolenoyl moieties of TAG can be used for the enrichment of this acid in the unhydrolyzed acylglycerol fractions of GLA‐containing oils.
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