(S)-carbonyl reductase II (SCRII), a short-chain alcohol dehydrogenase from Candida parapsilosis M203011, catalyzes the bioreduction of 2-hydroxyacetophenone (2-HAP) to (S)-1-phenyl-1,2-ethanediol ((S)-PED). When SCRII was expressed in Escherichia coli, the biotransformation efficiency of (S)-PED was low. To improve itstiocatalytic efficiency, the homologous expression of SCRII in C. parapsilosis M203011 was attempted. The scrII gene was cloned into an expression vector pCP carrying MAL2 as its promoter and SAT1 as its selection marker. Data obtained in this study showed that SCRII was successfully expressed in recombinant strain C. parapsilosis/pCP-scrII. The reductive activity toward 2-HAP exhibited about 2-fold and 6-fold increase in the cell-free extracts of C. parapsilosis/pCP-scrll than those of the wild-type and E. coli/pET28-SCRII. Under the optimal bioreaction conditions (pH 5.5, 35 degrees C), the optical purity and yield of (S)-PED were both over 99.9% produced by C. parapsilosis/pCP-scrll. Additionally, 500-mL preparative scale bioreduction with efficient whole-cell process was performed, and the optical purity was over 99.9% with an isolated yield of about 70%. Our work not only demonstrated the high catalytic efficiency given by the homologous expression of SCRII in C. parapsilosis, but also provides an economical method for the preparation of optically pure chiral alcohols with whole-cell process. (C) 2016 Elsevier Ltd. All rights reserved.