Abstract: A novel NADPH dependent carbonyl reductase was separated from Candida parapsilosis CCTCC 203011. The enzyme gave a single band on SDS-PAGE，which was purified through ammonium sulfate，DEAE Sepharose FF，Phenyl-Sepharose FF and Blue Sepharose FF chromatography from cell-free extract. The molecular mass of the enzyme was about 30kD. The optimum pH and temperature for reduction were 4.5 and 35℃ respectively. The Cu2+ had strong restrictive effect on enzyme activity. In addition，the carbonyl reductase was an enzyme with high substrate specificity and stereo-selectivity，and showed high asymmetric reduction activity towards α-hydroxyacetophenone and ethyl 4-chloro acetoacetate. For the asymmetric reduction of α-hydroxyacetophenone and ethyl 4-chloro acetoacetate，(S)-1-phenyl-1,2-ethanediol and (R)-ethyl 4-chloro-3-hydroxybutanoate were produced by the purified enzyme，with the 100% and 94.3% e.e value respectively. So the enzyme could be one of the effective biocatalysts for asymmetric synthesis of chiral alcohols. The amino acid sequences of one peptide from the purified enzyme were analyzed by LC-MASS-MASS，and the carbonyl reductase showed some identity to the hypothetical protein CaO19.10414 reported.