Crude palm oil (CPO) processing for sn-2 palmitate synthesis requires a specific sn-1,3 lipase to catalyze the hydrolysis step. These lipases are known to be derived from filamentous fungal isolates including Aspergillus niger and Rhizopus oryzae. The purpose of this study was to describe extracellular lipases from A. niger and R. oryzae that hydrolyze CPO. Extracellular lipases were successfully recovered from both fungal isolates using CPO-enriched fermentation media. The crude fraction was partially refined using (NH4)2SO4 and dialyzed, yielding two fractions. Lipase fraction I from both fungal species had the highest specific activity, had a molecular mass of ~30 kDa, and was sn-1,3 specific. The best conditions for enzyme activity of both fungal species in CPO hydrolysis were pH 6-7 and 35 ℃. The pH and heat stability of lipase fraction I in both fungi were relatively low. However, this enzyme worked effectively in benzene, ethanol, and methanol solvents.
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