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Partial purification and properties of lipase from germinating seeds of Jatropha curcas L.
Author(s) -
Abigor Roland D.,
Uadia Patrick O.,
Foglia Thomas A.,
Haas Michael J.,
Scott Karen,
Savary Brett J.
Publication year - 2002
Publication title -
journal of the american oil chemists' society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.512
H-Index - 117
eISSN - 1558-9331
pISSN - 0003-021X
DOI - 10.1007/s11746-002-0614-3
Subject(s) - lipase , jatropha curcas , chemistry , hydrolysis , food science , ammonium sulfate precipitation , ammonium , chromatography , botany , biochemistry , biology , enzyme , organic chemistry , size exclusion chromatography
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.