脂肪酶YCJ01拆分对位取代α-苯乙醇  

Asymmetric transesterification resolution of para-(R,S)-α-phenylethanol by lipase YCJ01

作　　者：秦燕[1] 李文豪[1] 汪斌[1] 何冰芳[1] 

机构地区：[1]南京工业大学生物与制药工程学院,江苏南京211800

出　　处：《生物加工过程》2015年第4期47-51,共5页Chinese Journal of Bioprocess Engineering

基　　金：国家高技术研究发展计划(863计划)重大项目(2012AA022205);国家重点基础研究发展计划(973计划)(2011CB710800)

摘　　要：利用脂肪酶YCJ01催化拆分对位取代α-苯乙醇衍生物。以异丙醚为反应介质,采用乙酸乙烯酯作为酰基供体,对180 mmol/L的1-(4-甲基苯基)乙醇进行选择性酯化,脂肪酶粗酶粉添加量为5 g/L,50℃反应21 h后,底物转化率可达49.96%,对映体过量值e.e.s、e.e.p值分别为97.1%和97.2%,对映体选择性E>200;同样,对1-(4-甲氧基苯基)乙醇进行选择性酯化,酰基供体为丁酸乙烯酯,底物浓度150 mmol/L,脂肪酶粗酶粉添加量为2.5g/L,30℃反应12 h后,底物转化率为49.8%,e.e.s、e.e.p值分别为97.7%和98.4%,对映体选择性E>200,显示了很好的手性拆分效果。Asymmetric transesterification resolution of para-（ R,S）-α-phenylethanol was conducted by lipase YCJ01. The resolution conditions of para-（ R,S）-α-phenylethanol were optimized. Reaction was carried out in isopropyl ether using vinyl acetate as acyl donors with 5 g / L lipase YCJ01 and 180 mmol /L 1-（ 4-methylphenyl） ethanol. The mixture was incubated at 50 ℃ for 21 h. After the reaction,the substrate conversion could reach 49. 96% with e. e.s= 97. 1%,e. e.p= 97. 2%,E 200. Similarly,high enantiomeric purity（ e. e.s= 97. 7%,e. e.p= 98. 4%,E 200） and substrate conversion（ 49. 82%） were achieved at 30 ℃ after 12 h in isopropyl ether with 2. 5 g / L lipase YCJ01 and 150 mmol / L 1-（ 4-methoxyphenyl） ethanol,vinyl butyrate as acyl donors. All results illustrated that lipase YCJ01 was an exploitable biocatalyst for chiral resolution of pharamaceutical intermediate.

关 键 词：耐有机溶剂脂肪酶 手性拆分 Burholderia ambifaria Α-苯乙醇 

分 类 号：Q814[生物学—生物工程]