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首页> 外文期刊>Catalysis science & technology >Hydroxynitrile lyases covalently immobilized in continuous flow microreactors
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Hydroxynitrile lyases covalently immobilized in continuous flow microreactors

机译：醇腈酶共价固定化连续流微反应器

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摘要

Enzymes are supreme catalysts when it comes to high enantiopurities and their immobilization will pave the way for continuous operation. In this context, we show the covalent immobilization of hydroxynitrile lyases HbHNL (from Hevea brasiliensis) and MeHNL (from Manihot esculenta) in a siliceous monolithic microreactor for continuous operation. A thorough characterization of the immobilized HNLs on mesoporous silicates indicated the conditions essential for a successful immobilization. Their application in a continuous flow system enabled a remarkably fast (3.2 min) production of chiral cyanohydrins with high conversion (97%) and high ee (98%) using minimal enzyme loading (STY = 71 g L-1 h(-1) mgprotein(-1)). MeHNL showed increased operational stability, possibly due to a structural difference. The continuous flow microreactor outperformed batch systems, demonstrating the advantage of the mesoporous/macroporous environment for the expression of enzyme activity and the favorable characteristics of the microreactor. Overall, the system shows great potential for future industrial application of biocatalytic asymmetric syntheses.
机译：酶是最高催化剂时高enantiopurities及其固定化将为连续操作铺平了道路。这种情况下,我们展示了共价固定化醇腈酶的HbHNL(从橡胶树从木薯取代巴西橡胶树)和MeHNL(耐)在硅质单片微反应器连续操作。介孔的固定化HNLs硅酸盐表示必不可少的一个条件成功的固定。连续流系统启用一个非常快(3.2分钟)手性氰醇的生产高转化率(97%)和高情感表达(98%)使用最小的酶加载(猪圈= 71 g l - 1 h (1)mgprotein(1))。操作稳定,可能由于结构的差异。微反应器优于批处理系统,展示的优势介孔/大孔的环境表达的酶活性和良好的微反应器的特性。系统展示了未来的巨大潜力工业应用biocatalytic不对称合成。

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