从蜡样芽孢杆菌WZY004 基因组DNA 中克隆获得了烯醇还原酶基因，并在大肠杆菌BL21（DE3）中以可溶形式过量表达。重组烯醇还原酶经Ni-NTA 亲和层析分离纯化后，对其酶学性质进行了详细表征。该重组酶经SDS-PAGE 检测为单一条带，其分子量为38.2 kD。该酶最适pH 和温度分别为7.5 与60 °C。对氧代异佛尔酮的Km和Vmax 值分别为1.83 mmol/L与1.13 U/mg。底物特异性分析表明该酶对柠檬醛、2-甲基-2-戊烯醛和反式-2-癸烯醛均有较高活力，其中对柠檬醛的比酶活高达1.33 U/mg。

The gene encoding an enoate reductase was cloned from the genomic DNA of Bacillus cereus WZY004 and over-expressed as a soluble protein in Escherichia coli BL21 (DE3). The recombinant enzyme was purified by Ni-NTA affinity chromatography and subsequently characterized. The SDS-PAGE analysis of the purified enzyme revealed a single band corresponding to the molecular weight of around 38.2 kD. The enzyme exhibited the maximum activity at pH 7.0 and
temperature 60 °C. The values of Km and Vmax for ketoisophorone were 1.83 mmol/L and 1.13 U/mg, respectively. In addition, the purified enzyme showed higher activity when citral, 2-methyl-2-pentenal or trans-2-decenal was used as substrate.