|Abigor, Roland - NIGERIAN INST|
|Uadia, Patrick - UNIV OF BENIN|
Submitted to: Journal of the American Oil Chemists' Society
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: October 20, 2001
Publication Date: May 20, 2002
Citation: ABIGOR, R.D., UADIA, P.O., FOGLIA, T.A., HAAS, M.J., SCOTT, K.M., SAVARY, B.J. PARTIAL PURIFICATION AND PROPERTIES OF LIPASE FROM GERMINATING SEEDS OF JATROPHA CURCAS L.. JOURNAL OF THE AMERICAN OIL CHEMISTS SOCIETY. 2002. v. 79. p. 1123-1126. Interpretive Summary: In developing countries such as Nigeria, most oleochemical products, such as fatty acids, are imported, which exacerbates the trade deficit and economic growth of developing countries. One way of addressing this problem is to use underutilized indigenous oil seed plants as a source of needed oleochemicals. In nature, intact oils and fats are broken down into fatty acids by a class of enzymes called lipases. Most oil seed-bearing plants produce their own lipases, which are specific for the fatty acids present in the seeds. This paper reports the isolation and partial characterization of the lipase present in the seeds of the shrub Jatropha curcas L, which is native to Nigeria. The shrub, which is widely grown, produces an abundance of seeds containing as much as 60% oil that is presently left to decompose on the ground. Application of the isolated lipase to these domestic oil seeds will facilitate the recovery of fatty acids for oleochemical use in Nigeria.
Technical Abstract: The lipase present in the seeds of Jatropha curcas L. was isolated, partially purified, and some of its properties studied. Lipase activity was detected in both the dormant and germinating seeds. The lipase hydrolysed palm kernel, coconut, and olive oils at comparable rates (approximately 5 µg FFA /µg protein/min) and hydrolysed palm, Raphia hookeri and Jatropha curcas L. oils at about twice the rate of the first group of oils. 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.