Carbonyl reductasese (CR) with the ability of aromatic ketone asymmetry reduction was extracted from red bean (CRrb) by grinding, centrifigation, filtration and acetone precipitation. CRrb liquid with 5.8 fold increase in purity was achieved by rapid purification, and its enzymatic properties were examined and compared with the microbe origin CR. CRrb was coupled with formate dehydrogenase (FDH) to construct a bi-enzyme system to continuously catalyse the reaction of b-hydroxyacetophenone to (R)-phenylethanediol. The results showed that the optimal reaction pH value of CRrb was 6.0, and the optimal reaction temperature of CRrb was 45℃. It showed higher thermostability between 40~60℃ than the microbe origin CR. The kinetics parameters (Michaelis constant Km and maximum reaction velocity Vmax) of CRrb were 5.68 mmol/L and 20.21 mmol/(min×mL) respectively, which indicate its affinity with the substrate and catalysis efficiency were higher than CR from microbe origin. Under the optimization reaction conditions of coupling system, the substrate tolerance concentration reached 60 mmol/L which was higher than the microbe origin CR. The reaction efficiency of the coupling system was the highest when the enzymatic activity rate of CRrb/FDH was optimized as 1:1.5, and the acquired production mol number when 1 mol cofactor was turned of coupling system batch reaction was improved from 266 mol to 365 mol.