Enzymatic resolution of α-tetralols by CALB-catalyzed acetylation
Enzymatic resolution of α-tetralols by CALB-catalyzed acetylation
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DOI：
10.1016/j.tetasy.2007.05.007
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发表时间：
2007-05-29
影响因子：
--
通讯作者：
Porto, Andre L. M.
中科院分区：
文献类型：
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作者：
Ferraz, Helena M. C.;Bianco, Graziela G.;Porto, Andre L. M.
以南极念珠菌脂肪酶（CALB-Novozym(R) 435）为生物催化剂，对外消旋四醇进行酯化反应，得到了一系列同手性α -四醇及其相应的乙酸酯。该酶被证明对所研究的底物具有很高的动力学分辨率，提供(+)-四醇醇和(+)-乙酸酯极好的对映体过量（高达>99%）和非常好的产率（>40%）。(C) 2007 Elsevier Ltd.版权所有。
A series of homochiral alpha-tetralols, as well as their respective acetates, has been obtained by esterification of racemic tetralols, using Candida antarctica lipase (CALB-Novozym(R) 435) as the biocatalyst. This enzyme is shown to be highly efficient for the kinetic resolution of the substrates studied, affording the (+)-tetralols and the (+)-acetates in excellent enantiomeric excess (up to >99%) and very good yields (>40%). (C) 2007 Elsevier Ltd. All rights reserved.