With pH, temperature and metal ions as the parameters, the lipolysis of olive oil in buffers via a partially purified Carica papaya lipase (pCPL) was investigated and compared with that via crude preparation (CPL). The lipase-catalyzed hydrolysis of (R,S)-naproxen thioester in water-saturated organic solvents was then employed as the other model system, in which pCPL was found to be superior to CPL and Candida rugosa lipase (CRL) when the enzyme activity, thermal stability, enantioselectivty and reuse of the recovered lipase was considered. Moreover, in the pCPL-catalyzed dynamic kinetic resolution of (R,S)-naproxen thioester, the concentration of trioctylamine added as a racemization catalyst was found to have profound effects on the kinetic constants for (R)- and (S)-thioester.