Lipase Covalently Attached to Multiwalled Carbon Nanotubes as an Efficient Catalyst in Organic Solvent
Lipase Covalently Attached to Multiwalled Carbon Nanotubes as an Efficient Catalyst in Organic Solvent
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DOI：
10.1002/aic.12180
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发表时间：
2010-11-01
期刊：
影响因子：
3.7
通讯作者：
Feng, Wei
中科院分区：
文献类型：
--
作者：
Ji, Peijun;Tan, Huishan;Feng, Wei
将脂肪酶共价连接到多壁碳纳米管上。通过圆二色谱和红外光谱分析了脂肪酶与碳纳米管连接后的结构变化。以正庚烷为反应介质，将该偶联物用于模型化合物（R，S）-1-苯基乙醇的拆分。酶促拆分在35至60 ℃的温度下进行。结果表明，连接到MWNTs上的脂肪酶显着影响酶的性能，在温度依赖性和分辨率效率。与天然脂肪酶相比，MWNT脂肪酶的活性具有较小的温度依赖性。多壁碳纳米管脂肪酶的拆分效率大大提高。MWNT脂肪酶保留了天然脂肪酶对（R）-1-苯基乙醇的选择性。连续使用表明，MWNT脂肪酶在拆分（R，S）-1-苯基乙醇中具有良好的稳定性。(C)2010美国化学工程师学会AIChE J，56：3005-3011，2010
Lipase was covalently attached to multiwalled carbon nanotubes (MWNTs). Structural changes of the lipase upon attachment onto MWNTs were analyzed through circular dichroism and FTIR spectroscopy. The conjugate was utilized for the resolution of a model compound (R,S)-1-phenyl ethanol, and the reaction medium was n-heptane. The enzymatic resolutions were carried out at temperatures from 35 to 60 degrees C. The results show that the lipase attached onto MWNTs has significantly affected the performance of the enzyme in terms of temperature dependence and resolution efficiency. The activity of MWNT lipase was less temperature-dependent compared with that of the native lipase. The resolution efficiency was much improved with MWNT lipase. MWNT lipase retained the selectivity of the native lipase for (R)-1-phenyl ethanol. The consecutive use of MWNT lipase showed that MWNT lipase had a good stability in the resolution of (R,S)-1-phenyl ethanol. (C) 2010 American Institute of Chemical Engineers AIChE J, 56: 3005-3011, 2010