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作 者:周昌平[1] 寇广会[1] 徐庆阳[1] 陈宁[1]
机构地区:[1]天津科技大学天津市工业微生物重点实验室,天津300457
出 处:《现代化工》2006年第z2期275-278,共4页Modern Chemical Industry
基 金:天津市科委应用基础研究重点基金项目(05YFJZJC00901)
摘 要:以DL-2-氨基-△2-噻唑啉-4-羧酸(DL-ATC)为转化底物,采用来自假单胞菌(Pseudomonas sp.)TS1138的L-半胱氨酸合成酶系对DL-ATC进行生物转化合成L-半胱氨酸.对转化条件进行了研究,得出TS1138菌株合成L-半胱氨酸的最适转化条件;反应温度为42~44℃,转化时间为2.5 h,底物质量浓度为6g/L,酶源细胞浓缩倍数为5倍.动力学研究表明,TS1138菌株L-半胱氨酸合成酶系的米氏常数(Km)为7.1 997 mmol/L,最大初反应速度Vmax=41.6629 mmol/(L·min).L-cysteine was produced from DL-2-aminoΔ~2-thiazoline-4-carboxylic acid(DL-ATC) by means of microbial transformation in the presence of L-cysteine synthesizing enzyme from Pseudomonas sp.TS1138.Conditions for bio-transformation were studied,and the optimum conditions were as follows,transformation temperature was 42-44℃,transformation time was 2.5 h,mass concentration of DL-ATC was 6 g/L,concentration times of enzyme was 5.Kinetic studies showed that Michaelis constant(K_m) of Lcysteine synthesizing enzyme from Pseudomonas sp.TS1138 is 7.1997 mmol/L and maximal reaction rate(V_(max)) is 41.6629 mmol/(L·min).
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