Partial purification and properties of lipase from germinating seeds of Jatropha curcas L

Lipase present in the seeds of Jatropha curcas L. was isolated and some of its properties studied. Lipase activity was detected in both dormant and germinating seeds. The lipase was partially purified using a combination of ammonium sulfate precipitation and ultrafiltration, which increased the rela...

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Bibliographic Details
Published in:Journal of the American Oil Chemists' Society Vol. 79; no. 11; pp. 1123 - 1126
Main Authors: Abigor, Roland D., Uadia, Patrick O., Foglia, Thomas A., Haas, Michael J., Scott, Karen, Savary, Brett J.
Format: Journal Article
Language:English
Published: Berlin/Heidelberg Springer-Verlag 01-11-2002
Springer
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Summary:Lipase present in the seeds of Jatropha curcas L. was isolated and some of its properties studied. Lipase activity was detected in both dormant and germinating seeds. The lipase was partially purified using a combination of ammonium sulfate precipitation and ultrafiltration, which increased the relative activity of the lipase by 28‐ and 80‐fold, respectively. The lipase hydrolyzed palm kernel, coconut, and olive oils at comparable rates (approximately 5 μg FFA/μg protein/min); palm—Raphia hookeri and Jatropha curcas L.—oils at about twice the rate of the first group of oils; and palm and fish oils at a higher rate than all other oils. The lipase, however, had the highest activity with monoolein. Optimal pH and temperature for maximal lipase activity were 7.5 and 37°C, respectively. The addition of ferric ion (15 mM) to the lipase assay medium caused 90% inhibition of lipase activity, whereas calcium and magnesium ions enhanced lipase activity by 130 and 30%, respectively.
ISSN:0003-021X
1558-9331
DOI:10.1007/s11746-002-0614-3