A novel 2-aminoacetophenone reductase was purified to homogeneity from Arthrobacter sulfureus BW1010. The enzyme is a monomer with a molecular weight of approximately 60 kDa. Using NADPH as coenzyme, it catalyzes the reduction of ketones, especially amine phenyl ketones, and stereospecifically reduces 2-aminoacetophenone to (S)-2amino-1-phenylethanol (e.e > 99.8%) with the optimal pH at 7.5. (C) 2014, The Society for Biotechnology, Japan. All rights reserved.