利用色氨酸酶酶法拆分D,L-丝氨酸制备D-丝氨酸  

Preparation of D-Serine by Enzymatic Resolution of D,L-Serine Using Tryptophanase

作　　者：丁国钰[1] 彭佳敏[1] 郭婷婷[1] 高智慧 

机构地区：[1]南开大学药学院天津市分子药学重点实验室,天津300071 [2]天津启仁医药科技有限公司,天津300457

出　　处：《精细化工》2012年第10期947-951,共5页Fine Chemicals

基　　金：天津市科技计划项目(09ZCKFSH00900)~~

摘　　要：以D,L-丝氨酸为底物,采用色氨酸酶将L-丝氨酸转化为L-色氨酸,并进一步分离纯化拆分得到D-丝氨酸。该文对色氨酸酶酶法拆分条件进行了响应面优化,酶促反应最佳条件为:温度45℃,pH=8.0,反应时间18 h,底物D,L-丝氨酸质量浓度30 g/L,色氨酸酶用量为6 g/L,经过两次转化,L-丝氨酸的总转化率可达95.4%。酶促反应液经NKA-Ⅱ型大孔吸附树脂与001×7强酸性阳离子交换树脂纯化,重结晶后得到D-丝氨酸,化学纯度99.4%,α2D0=-15.3°(ρ=0.1 kg/L,2 mol/L HCl),总回收率为66.6%。A practical method was established to resolve L-serine into L-tryptophan via tryptophanase,using D,L-serine as substrate.D-Serine could be obtained by further isolation and purification.Response surface methodology was used to optimize the conditions of the enzymatic resolution.And the optimum conditions were：45 ℃,pH 8.0,18 hours,30 g/L of substrate mass concentration and 6 g/L of tryptophanase mass concentration.After two similar reactions,the total conversion rate of L-serine could be up to 95.4%.The products were separated and purified on NKA-Ⅱ macroporous absorption resin and 001×7 ion-exchange resin and then recrystallized to give D-serine,the purity of which was 99.4%.The optical rotation of D-serine was-15.3°（ρ=0.1 kg/L,2 mol/L HCl） and the total separation recovery of the products was 66.6%.

关 键 词：D-丝氨酸 酶法拆分 色氨酸酶 响应面分析 分离提纯技术 

分 类 号：TQ217[化学工程—有机化工]