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酶法合成L—丝氨酸及反应液中氨基酸的分离[J]. 中国药科大学学报, 2000, (2): 57-60.
引用本文: 酶法合成L—丝氨酸及反应液中氨基酸的分离[J]. 中国药科大学学报, 2000, (2): 57-60.
Enzymatic Production of L Serine and Separation of Amino Acids from Reaction Solution[J]. Journal of China Pharmaceutical University, 2000, (2): 57-60.
Citation: Enzymatic Production of L Serine and Separation of Amino Acids from Reaction Solution[J]. Journal of China Pharmaceutical University, 2000, (2): 57-60.

酶法合成L—丝氨酸及反应液中氨基酸的分离

Enzymatic Production of L Serine and Separation of Amino Acids from Reaction Solution

  • 摘要: 含glyA的基因工程菌所表达的SHMT可催化甲醛和甘氨酸特异地合成L-丝氨酸。对酶法合成的部分条件进行了优化,并根据甲醛滴定的原理,确定了通过检测pH变化控制甲醛流加速度的方案,最终的反应液中L-丝氨酸浓度达0.2mol/L。反应结束后的酶反应液中同时含有甘氨酸和丝氨酸,利用国产717树脂获得较为理想的分离效果,丝氨酸的收率达77%,高效液相分析表明其中不含甘氨酸等杂质。

     

    Abstract: Serine hydromethyltransferase (SHMT) expressed by genetic engineered bacteria can synthesize L serine from HCHO and glycine. Some reaction conditions were optimized. Based on the principle of HCHO titration, the feed rate of HCHO solution was controlled

     

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