Lipase was covalently attached to multiwalled carbon nanotubes (MWNTs). Structural changes of the lipase upon attachment onto MWNTs were analyzed through circular dichroism and FTIR spectroscopy. The conjugate was utilized for the resolution of a model compound (R,S)-1-phenyl ethanol, and the reaction medium was n-heptane. The enzymatic resolutions were carried out at temperatures from 35 to 60 degrees C. The results show that the lipase attached onto MWNTs has significantly affected the performance of the enzyme in terms of temperature dependence and resolution efficiency. The activity of MWNT lipase was less temperature-dependent compared with that of the native lipase. The resolution efficiency was much improved with MWNT lipase. MWNT lipase retained the selectivity of the native lipase for (R)-1-phenyl ethanol. The consecutive use of MWNT lipase showed that MWNT lipase had a good stability in the resolution of (R,S)-1-phenyl ethanol. (C) 2010 American Institute of Chemical Engineers AIChE J, 56: 3005-3011, 2010