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

被引：145

作者：

Hu, Bin ^{[1
]}

Pan, Jiang ^{[1
]}

Yu, Hui-Lei ^{[1
]}

Liu, Jian-Wen ^{[1
]}

Xu, Jian-He ^{[1
]}

机构：

[1] E China Univ Sci & Technol, State Key Lab Bioreactor Engn, Lab Biocatalysis & Bioproc, Shanghai 200237, Peoples R China

来源：

PROCESS BIOCHEMISTRY | 2009年 / 44卷 / 09期

基金：

中国国家自然科学基金;

关键词：

Lipase; Immobilization; Magnetic nanoparticles; Enzymatic biocatalytic resolution; Diltiazem intermediate; Biphasic reaction; ENANTIOSELECTIVE HYDROLYSIS; ENZYMES; RESOLUTION; ESTER;

D O I：

10.1016/j.procbio.2009.05.001

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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. (C) 2009 Elsevier Ltd. All rights reserved.

引用

页码：1019 / 1024

页数：6

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