Immobilized lipase screening towards continuous-flow kinetic resolution of (±)-1,2-propanediol

被引:22
作者
Aguillon, Anderson R. [1 ]
Avelar, Marcelo N. [1 ]
Gotardo, Larissa E. [1 ]
de Souza, Stefania P. [1 ]
Leao, Raquel A. C. [1 ,2 ]
Itabaiana Jr, Ivaldo [3 ]
Miranda, Leandro S. M. [1 ]
de Souza, Rodrigo O. M. A. [1 ,2 ]
机构
[1] Univ Fed Rio de Janeiro, Chem Inst, Biocatalysis & Organ Synth Grp, BR-21941909 Rio De Janeiro, Brazil
[2] Univ Fed Rio de Janeiro, Fac Farm, BR-21941170 Rio De Janeiro, RJ, Brazil
[3] Univ Fed Rio de Janeiro, Sch Chem, Dept Biochem Engn, BR-21941910 Rio De Janeiro, RJ, Brazil
关键词
Lipase; Continuous-flow; Kinetic resolution; BROMIDE-CATALYZED REACTION; ASYMMETRIC HYDROGENATION; RACEMIC PROPANE-1,2-DIOL; TERMINAL EPOXIDES; PACKED-BED; DIOLS; ENANTIOSELECTIVITY; ETHERIFICATION; ALCOHOLS; 1,2-DIOL;
D O I
10.1016/j.mcat.2019.01.034
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
Here, we report a flow chemistry approach for kinetic resolution of (+/-)-1,2-propanediol protected by trityl group using the packed-bed reactor filled with different immobilized enzymes. It was investigated the performance of 16 immobilized lipases, including commercial Lipozyme TL, Novozym 51032, Novozym 435 (N435) and lipases immobilized by our group. Based on the values of conversion and enantioseletivity, batch experiments were then translated to the continuous-flow environment. Continuous flow (CF) reactors allowed reaction time reduction, from 6 h in batch to 7 min, keeping the values of conversion (up to 50%) and selectivity (E value > 200) during the reaction procedure using the commercial enzyme Novozym 435. In addition, continuous flow conditions increased the productivity of kinetic resolution 3 times when compared to conventional batch reactor, after its optimization.
引用
收藏
页码:128 / 134
页数:7
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