文献类型：期刊文献

英文题名：Immobilization of Serratia marcescens lipase onto amino-functionalized magnetic nanoparticles for repeated use in enzymatic synthesis of Diltiazem intermediate

作者：Hu, Bin[1]; Pan, Jiang[1]; Yu, Hui-Lei[1]; Liu, Jian-Wen[1]; Xu, Jian-He[1]

机构：[1] State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 130 Meilong Road, Shanghai, 200237, China

年份：2009

卷号：44

期号：9

起止页码：1019

外文期刊名：Process Biochemistry

收录：EI(收录号：20092912201604)

语种：英文

外文关键词：Nanoparticles - Proteins - High resolution transmission electron microscopy - Reaction intermediates - Fourier transform infrared spectroscopy - Magnetite - Coprecipitation - Nanomagnetics - Synthesis (chemical)

摘要：Magnetic Fe3O4 nanoparticles were prepared by chemical coprecipitation method and subsequently coated with 3-aminopropyltriethoxysilane (APTES) via silanization reaction. The synthesized materials were characterized by transmission electron microscopy (TEM) and Fourier transform infrared spectroscopy (FTIR). With glutaraldehyde as the coupling agent, the lipase from Serratia marcescens ECU1010 (SmL) was successfully immobilized onto the amino-functionalized magnetic nanoparticles. The results showed that the immobilized protein load could reach as high as 35.2 mg protein g-1 support and the activity recovery was up to 62.0%. The immobilized lipase demonstrated a high enantioselectivity toward (+)-MPGM (with an E-value of 122) and it also displayed the improved thermal stability as compared to the free lipase. When the immobilized lipase was employed to enantioselectively hydrolyze (±)-trans-3-(4-methoxyphenyl)glycidic acid methyl ester [(±)-MPGM] in water/toluene biphasic reaction system for 11 consecutive cycles (totally 105 h), still 59.6% of its initial activity was retained, indicating a high stability in practical operation. ? 2009 Elsevier Ltd. All rights reserved.