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固定化脂肪酶于氨基环糊精功能化碳纳米管上,在离子液体-有机溶剂界面进行酶催化反应。

Immobilization of lipase on amino-cyclodextrin functionalized carbon nanotubes for enzymatic catalysis at the ionic liquid-organic solvent interface.

机构信息

Department of Biochemical Engineering, Beijing University of Chemical Technology, Beijing, China.

出版信息

Colloids Surf B Biointerfaces. 2013 Feb 1;102:124-9. doi: 10.1016/j.colsurfb.2012.07.050. Epub 2012 Aug 14.

DOI:10.1016/j.colsurfb.2012.07.050
PMID:23010110
Abstract

Amino-cyclodextrin was covalently attached to multiwalled carbon nanotubes (MWNTs). The functionalized MWNTs have a good dispersibility in water. The lipase was adsorbed onto the functionalized MWNTs. The immobilized lipase was utilized for the resolution of the model compound (R, S)-1-phenyl ethanol in heptane, the ionic liquid [Bmim]PF(6) as well as the heptane/[Bmim]PF(6) mixture. In the reaction media, the enzymatic activity of the immobilized lipase is much higher than that of the native lipase. In comparison to the catalysis in the ionic liquid and heptane, when using the mixture of heptane/[Bmim]PF(6) as the reaction medium, the catalysis by the immobilized lipase at the heptane-ionic liquid interface exhibited a higher catalysis activity. This is due to two aspects: the continuous diffusion of substrate from the heptane phase to the ionic liquid phase; the simultaneous extraction of product from the ionic liquid phase. In addition, the interfacial enzymatic catalysis facilitates the reuse of the immobilized lipase and the ionic liquid.

摘要

氨甲基环糊精被共价键合到多壁碳纳米管(MWNTs)上。功能化的 MWNTs 在水中具有良好的分散性。脂肪酶被吸附到功能化的 MWNTs 上。固定化的脂肪酶用于拆分模型化合物(R,S)-1-苯乙醇在庚烷、离子液体[Bmim]PF(6)以及庚烷/[Bmim]PF(6)混合物中的反应。在反应介质中,固定化脂肪酶的酶活性远高于天然脂肪酶。与在离子液体和庚烷中的催化相比,当使用庚烷/[Bmim]PF(6)混合物作为反应介质时,固定化脂肪酶在庚烷-离子液体界面处的催化表现出更高的催化活性。这归因于两个方面:底物从庚烷相连续扩散到离子液体相;产物同时从离子液体相萃取。此外,界面酶催化有利于固定化脂肪酶和离子液体的重复使用。

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