期刊
CHEMISTRY-A EUROPEAN JOURNAL
卷 28, 期 60, 页码 -出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/chem.202202437
关键词
dynamic kinetic resolution; immobilization; lipases; mesoporous silica; propargyl alcohol; racemization
资金
- JSPS KAKENHI [18HO4411, 18H02556, 21H02605, 18KK0154]
- Research Support Project for Life Science and Drug Discovery (Basis for Supporting Innovative Drug Discovery and Life Science Research (BINDS)) from AMED [22ama121054]
In this study, a method for obtaining S enantiomers from secondary 3-(trialkylsilyl)propargyl alcohols was achieved by using a well-known R-selective Pseudomonas fluorescens lipase in combination with a racemization catalyst VMPS4, in which the silyl group reverses the size relationship of substituents near the carbinol moiety. Immobilization of the lipase on Celite was found to be important for achieving a high efficiency of the dynamic kinetic resolution.
Natural lipases typically recognize enantiomers of alcohols based on the size differences of substituents near the carbinol moiety and selectively react with the R enantiomers of secondary alcohols. Therefore, lipase-catalyzed dynamic kinetic resolution (DKR) of racemic secondary alcohols produces only R enantiomers. We report herein a method for obtaining S enantiomers by DKR of secondary 3-(trialkylsilyl)propargyl alcohols by using a well-known R-selective Pseudomonas fluorescens lipase in combination with a racemization catalyst VMPS4, in which the silyl group reverses the size relationship of substituents near the carbinol moiety. We have already reported R-selective DKR of the corresponding propargyl alcohols without substituents on the ethynyl terminal carbon, and the presence of an easily removable silyl group has enabled us to produce both enantiomers of propargyl alcohols in high chemical yields and with high enantiomeric excess. In addition, immobilization of the lipase on Celite was found to be important for achieving a high efficiency of the DKR.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据