Jatropha curcas L. is one of the seed plants that have lipase activity and can work well in hydrolysis reactions and chemical synthesis. This study aims to determine lipase activity that reacts with castor oil in organic solvents. In this research, organic solvents, especially hydrophobic solvents, were used in the hydrolysis reaction to increase lipase's catalytic activity. The organic solvent used has a hydrophobicity level between 2 and 4, namely hexane. The research stages consisted of lipase isolation, lipase assay, the effect of adding metal ions assay, and analysis of the compound of castor oil. The results showed that jatropha seeds had lipase activity in crude of 0.603 U/mL and increased to 0.911 U/mL after the addition of K+. The result of hydrolysis and transesterification of castor oil by lipase is ricinoleic acid (4,58%) and methyl ricinoleic (11,67%), and the concentration of ricinoleic acid (17.09%) and methyl ricinoleic (60.83%) were increased after addition of K+. The esterification reaction produces alkyl ester compounds such as methyl palmitate, ethyl pentadecanoate, methyl linoleate, methyl oleate, and methyl stearate. The lipase isolated from jatropha seeds not only catalyzes the hydrolysis reaction but also catalyzes chemical synthesis reactions such as esterification and transesterification.
Lipases are versatile enzymes with high specificity toward lipid substrate. They have many industrial applications, such as in food, pharmacy, and green fuel. So far, most explored lipases are from microbial and animal sources, whereas those from plants are less studied. The present study aims to characterize ketapang (Terminalia catappa Linn) lipase. The lipase was isolated from germinating ketapang seeds. The activity was determined by hydrolysis of virgin coconut oil (VCO). Biochemical characterization of ketapang lipase includes the optimum temperature, pH, kinetics, metal ions addition, and analysis of substrate specificity. It was shown that ketapang lipase has an optimum temperature of 45 oC, pH 7.5. Ca2+ increases the lipase activity, whereas Na+, K+, Mg2+, Zn2+, Fe2+, and Cu2+ inhibit ketapang lipase to various extents. A comparison of SDS-PAGE and native-PAGE analysis showed that ketapang lipase consists of several protein subunits. A further test by in-gel assay revealed that the 54 kDa, 35 kDa, two bands at ~16 kDa, and 12 kDa proteins showed lipolytic activity against a-naphthyl palmitate substrate. When tested on various chromogenic fatty acid substrates, ketapang lipase showed the highest specificity against short-chain fatty acids (C4 and C8), despite the fact that ketapang oil seed composes mainly of long fatty acid (C18). Since lipases that have high lipolytic activity toward short fatty acids are considered esterases, the esterase activity of ketapang lipase is yet to be determined.
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