Effect of lipase immobilization on resolution of (R, S)-2-octanol in nonaqueous media using modified ultrastable-Y molecular sieve as support
Effect of lipase immobilization on resolution of (R, S)-2-octanol in nonaqueous media using modified ultrastable-Y molecular sieve as support
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DOI：
10.1385/abab:134:1:39
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发表时间：
2006-07-01
影响因子：
3
通讯作者：
Xia, Liming
中科院分区：
文献类型：
--
作者：
Dai, Dazhang;Xia, Liming
将扩展青霉PED-03（PEL）脂肪酶固定化在改性超稳Y（USY）分子筛上，并在非水介质生物反应器中进行了（R，S）-2-辛醇的拆分。结果表明，改性USY分子筛负载的PEL催化拆分反应的转化率、对映体过量值（ee）和对映体选择性值（E）均远高于自由态和其它载体负载的PEL催化拆分反应的转化率、对映体过量值和对映体选择性值。改性USY分子筛固定化后的酶在较宽的pH范围内和较高的温度下均表现出明显的活性，且对热失活的稳定性显著提高，可“记忆”固定化缓冲液的适宜pH。改性USY分子筛固定化的PEL在非水介质中，pH 9.5，50 ℃，反应24 h，转化率达48.84%，具有良好的对映选择性（8批平均E值> 460），在光学纯（R，S）-2-辛醇的生产中具有良好的应用潜力。
The lipase from Penicillium expansum PED-03 (PEL) was immobilized onto modified ultrastable-Y (USY) molecular sieve and the resolution of (R, S)-2-octanol was carried out in a bioreactor in nonaqueous media by the immobilized lipase. It was found that the conversion rate, enantiomeric excess (ee) value, and enantioselectivity (E) value of the resolution catalyzed by PEL immobilized on modified USY molecular sieve were much higher than those of the reaction catalyzed by free PEL and PEL immobilized on other supports. Immobilized on modified USY molecular sieve, the PEL exhibited obvious activity within a wider pH range and at a much higher temperature and showed a markedly enhanced stability against thermal inactivation, by which the suitable pH of the buffer used for immobilization could be "memorized." The conversion rate of the reaction catalyzed by PEL immobilized on modified USY molecular sieve reached 48.84%, with excellent enantioselectivity (average E value of eight batches > 460) in nonaqueous media at "memorial" pH 9.5, 50 degrees C for 24 h, demonstrating a good application potential in the production of optically pure (R, S)-2-octanol.