Immobilization of Penicillin G Acylase on Magnetic Nanoparticles Modified by Ionic Liquids

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	Immobilization of Penicillin G Acylase on Magnetic Nanoparticles Modified by Ionic Liquids
	Zhou Huacong 1,2; Li Wei 1; Shou Qinghui 1,2; Gao Hongshuai 1; Xu Peng 1,2; Deng Fuli 1,2; Liu Huizhou 1
刊名	CHINESE JOURNAL OF CHEMICAL ENGINEERING
	2012-02-01
卷号	20 期号:1 页码:146-151
关键词	magnetic iron oxide magnetic nanoparticles ionic liquids penicillin G acylase enzyme immobilization
ISSN号	1004-9541
通讯作者	Li, W
英文摘要	Functionalized ionic liquids containing ethyoxyl groups were synthesized and immobilized on magnetic silica nanoparticles (MSNP) prepared by two steps, i.e., Fe3O4 synthesis and silica shell growth on the surface. This magnetic nanoparticle supported ionic liquid (MNP-IL) were applied in the immobilization of penicillin G acylase (PGA). The MSNPs and MNP-ILs were characterized by the means of Fourier transform infrared spectroscopy (FTIR), scanning electron microscopy (SEM), transmission electron microscopy (TEM), and vibrating sample magnetometer (VSM). The results showed that the average size of magnetic Fe3O4 nanoparticles and MSNPs were similar to 10 and similar to 90 nm, respectively. The saturation magnetizations of magnetic Fe3O4 nanoparticles and MNP-ILs were 63.7 and 26.9 A.m(2).kg(-1), respectively. The MNP-IL was successfully applied in the immobilization of PGA. The maximum amount of loaded enzyme was about 209 mg.g(-1) (based on carrier), and the highest enzyme activity of immobilized PGA (based on ImPGA) was 261 U.g(-1). Both the amount of loaded enzyme and the activity of ImPGA are at the same level of or higher than that in previous reports. After 10 consecutive operations, ImPGA still maintained 62% of its initial activity, indicating the good recovery property of ImPGA activity. The ionic liquid modified magnetic particles integrate the magnetic properties of Fe3O4 and the structure-tunable properties of ionic liquids, and have extensive potential uses in protein immobilization and magnetic bioseparation. This work may open up a novel strategy to immobilize proteins by ionic liquids.
WOS标题词	Science & Technology ; Technology
类目[WOS]	Engineering, Chemical
研究领域[WOS]	Engineering
关键词[WOS]	PHYSICAL-PROPERTIES ; STABILIZATION ; MICROSPHERES ; BIOCATALYST ; PARTICLES ; STABILITY ; LIPASE
收录类别	SCI
语种	英语
WOS记录号	WOS:000301011200021
公开日期	2013-10-25
内容类型	期刊论文
版本	出版稿
源URL	[http://ir.ipe.ac.cn/handle/122111/4283]
专题	过程工程研究所_生化工程国家重点实验室
作者单位	1.Chinese Acad Sci, State Key Lab Biochem Engn, Lab Green Proc & Engn, Inst Proc Engn, Beijing 100190, Peoples R China 2.Chinese Acad Sci, Grad Univ, Beijing 100049, Peoples R China
推荐引用方式 GB/T 7714	Zhou Huacong,Li Wei,Shou Qinghui,et al. Immobilization of Penicillin G Acylase on Magnetic Nanoparticles Modified by Ionic Liquids[J]. CHINESE JOURNAL OF CHEMICAL ENGINEERING,2012,20(1):146-151.
APA	Zhou Huacong.,Li Wei.,Shou Qinghui.,Gao Hongshuai.,Xu Peng.,...&Liu Huizhou.(2012).Immobilization of Penicillin G Acylase on Magnetic Nanoparticles Modified by Ionic Liquids.CHINESE JOURNAL OF CHEMICAL ENGINEERING,20(1),146-151.
MLA	Zhou Huacong,et al."Immobilization of Penicillin G Acylase on Magnetic Nanoparticles Modified by Ionic Liquids".CHINESE JOURNAL OF CHEMICAL ENGINEERING 20.1(2012):146-151.