Enhancement of the catalytic activity and stability of immobilized aminoacylase using modified magnetic Fe3O4 nanoparticles

被引：81

作者：

Feng, Junchen ^{[1
]}

Yu, Siran ^{[1
]}

Li, Jian ^{[2
]}

Mo, Ting ^{[1
]}

Li, Ping ^{[1
]}

机构：

[1] Tongji Univ, Sch Life Sci & Technol, Shanghai 200092, Peoples R China

[2] Anhui Agr Univ, Sch Engn, Hefei 230036, Peoples R China

来源：

CHEMICAL ENGINEERING JOURNAL | 2016年 / 286卷

基金：

中国国家自然科学基金; 国家高技术研究发展计划(863计划);

关键词：

Magnetic iron oxide (Fe3O4) nanoparticles; Aminoacylase; Immobilization; Covalent bond; LIPASE; GLUTARALDEHYDE; XYLANASE; SHELL;

D O I：

10.1016/j.cej.2015.10.083

中图分类号：

X [环境科学、安全科学];

学科分类号：

08 ; 0830 ;

摘要：

Aminoacylase (EC 3.5.1.14) was immobilized via covalent bonding to magnetic iron oxide (Fe3O4) nanoparticles with 3-(aminopropyl)triethoxysilane (APTES) modification. Magnetic Fe3O4 nanoparticles were prepared by chemical co-precipitation, controlling n(Fe3+):n(Fe2+) = 2:1 and c(Fe3+) + c(Fe2+) = 0.3 mol/L. The nanoparticles modified with APTES were characterized by SEM and FT-IR. The results showed that the optimal nanoparticle concentration, glutaraldehyde concentrations, crosslink time and immobilization time are 8 mg/mL, 1.0%, 1 h, and 1.5 h, respectively. Moreover, the optimal temperature, pH and thermostability of free and immobilized enzymes were compared. The properties of repeatedly used immobilized aminoacylase were also investigated. (C) 2015 Elsevier B.V. All rights reserved.

引用

页码：216 / 222

页数：7

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