乙酰鸟氨酸脱乙酰酶固定化细胞拆分D,L-缬氨酸  

Chiral Resolution of D,L-Valine by Immobilized Cells with Acetylornithine Deacetylase Activity

作　　者：张飞[1,2] 熊吉滨[1] 刘均忠[1] 刘鹏刚[1] 焦庆才[1] 

机构地区：[1]南京大学生命科学学院,医药生物技术国家重点实验室,南京210093 [2]包头轻工职业技术学院生物工程系,包头014043

出　　处：《高等学校化学学报》2009年第8期1577-1580,共4页Chemical Journal of Chinese Universities

基　　金：国家技术创新基金(批准号:02CJ-13-01-16)资助

摘　　要：报道了一种利用具有乙酰鸟氨酸脱乙酰酶活性的固定化细胞拆分D,L-缬氨酸的新方法. 该酶促反应最适条件： pH=6, 反应温度50 ℃, 底物N-乙酰-D,L-缬氨酸浓度200 mmol/L, 固定化细胞用量0.2 g/mL（或100 U/mL）. 0.1 mmol/L CoCl2条件对该酶促反应有显著的激活作用. 在以上条件下反应2～3 h, 测得产物L-缬氨酸浓度95 mmol/L. 该固定化细胞连续10次使用, 平均转化率为90.8%（以N-乙酰-L-缬氨酸计）, 显示出了良好的工业化应用前景.D-Amino acids are widely used intermediates in pharmacy. D-Amino acids can be produced by chiral separation of D,L-amino acids racemate. The stereospecific hydrolysis of N-acetyl-D, L-amino acids by microbial enzymys is one of the most extensively used procedures in optical resolution of D,L-amino acids. In this report, a new method of chiral resolution of D,L-valine by immobilized cells with acetylornithine deacetylase activity was developed. The optimum reaction conditions were 200 mmol/L N-acetyl-D, L-valine and 0. 2 g/mL（or 100 U/mL） of immobilized cells with 0. 1 mmol/L CoCl2 as activator at pH = 6. After 2--3 h incubation at 50 ℃, 95 mmol/L L-valine was obtained. In continuous use of immobilized cells for 10 times, the average conversion rate against N-acetyl-L-valine was 90.8%. The results display great potential in industrialization. This is the first report of chiral resolution of D,L-valine by acetylornithine deacetylase（ArgE）.

关 键 词：乙酰鸟氨酸脱乙酰酶 拆分 固定化细胞 D L-缬氨酸 

分 类 号：O629.71[理学—有机化学]