中文摘要：

在有氧条件下，利用DEAE Sepharose Fast Flow弱阴离子离子交换层析和Blue Sepharose CL-6B亲和层析，同时分离并提纯克雷伯杆菌胞内的1，3-丙二醇氧化还原酶和甘油脱氢酶．研究表明，1，3-丙二醇氧化还原酶的纯化倍数为35．86倍，回收率为5．17％，该酶最适表观反应温度为57℃，最适反应pH值为9．5．在30℃及pH-8．0～10．0时，该酶具有良好的稳定性．在45℃和pH-9．5条件下，该酶以1，3-丙二醇和NAD^＋为底物，其米氏常数K。分别为15．8，0．2mmol·L_。．1，3一丙二醇氧化还原酶对生理反应底物3-羟基丙醛活性最大，对其他醇类也有氧化能力．Mn^2＋对酶有显著激活作用，巯基保护剂能明显提高酶的活力．

英文摘要：

1,3-propanediol oxidoreductase from Klebsiella pneumoniae was purified by DEAE sepharose fast flow ionexchange chromatography and Blue Sepharose CL-6B affinity chromatography under aerobic conditions. A 35. 86-fold purification was obtained with the recovery of 5. 17 % activity. The optimum temperature and pH of the enzyme activity were 57 ℃ and 9.5 of pH value. At 30 ℃ and at range of pH 8. 0～10. 0, 1,3-propanediol oxidoreductase was stable. At 45 ℃ and pH 9. 5 the Km for 1,3-propanediol and NAD^＋ were 15.8 mmol · L^-1 and 0. 2 mmol · L^-1, respectively. The enzyme oxidized other alcohols such as pentanol, propanol, ethylene glycol and 1,4-butanediol, besides physiological substrate 3- hydroxypropionaldehyde. The enzyme was significantly activated by Mn^2＋. Reducing agents were able to enhence the activity of 1,3-propanediol oxidoreduetase.