A comparative studies of partial purified lipase from different maturity stages of oil palm mesocarp (E. guineensis var. Tenera)

Lipase is a triacylglycerol-hydrolyzing enzyme which is catalyzed the hydrolysis of water insoluble free fatty acids and. The whole protein extraction process was conducted at 4°C and in a sterile manner. Mesocarp of the oil palm is used to extract lipase. The presence of lipase in crude protein is determined by plate agar with tributyrin as substrate. Purification step was done by size-exclusion chromatography. The molecularweight of partial purified lipase was determined by SDS-PAGE. Titration with NaOH was used to conduct lipase assay and applied to find out the enzyme characterization. The optimum pH range for activity of lipase was alkaline pH,ranges, about pH 8.0 and 9.0. The optimum temperature was 40°C. In the presence of metal ions, some additives sharply decreased enzyme activity while some additives does not affect the enzyme activity. Lipase activity increase significantly in presence of CaCl₂ and MgCl₂. Low concentration of CaCl₂ increases the lipase activity but when increased to 50mM, its activity reduce sharply. Approximate molecular mass of partially purified enzyme was between 45kDa and 66.2kDa. It was found that lipase activity from over ripe oil palm is slightly higher compared ripe oil palm.