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Title 

Synthesis of Fe3O4@nickel?silicate core?shell nanoparticles for His-tagged enzyme immobilizing agents

 

히시티딘 태그된 효소 고정화를 위한 코에셀 나노파티클 합성

Authors 

M K ShinB KangNam Kyung YoonM H KimJ KiS HanJungoh AhnS Haam

Publisher 

Institute of Physics

Issue Date 

2016

Citation 

Nanotechnology, vol. 27, no. 49, pp. 495705-495705

Keywords 

cleavageenzyme immobilizationHis-tagnickel silicate covered superparamagnetic nanoparticleTEV protease

Abstract 

Immobilizing enzymes on artificially fabricated carriers for their efficient use and easy removal from reactants has attracted enormous interest for decades. Specifically, binding platforms using inorganic nanoparticles have been widely explored because of the benefits of their large surface area, easy surface modification, and high stability in various pH and temperatures. Herein, we fabricated Fe3O4 encapsulated 'sea-urchin' shaped nickel-silicate nanoparticles with a facile synthetic route. The enzymes were then rapidly and easily immobilized with poly-histidine tags (His-tags) and nickel ion affinity. Porous nickel silicate covered nanoparticles achieved a high immobilization capacity (85 μg mg-1) of His-tagged tobacco etch virus (TEV) protease. To investigate immobilized TEV protease enzymatic activity, we analyzed the cleaved quantity of maltose binding protein-exendin-fused immunoglobulin fusion protein, which connected with the TEV protease-specific cleavage peptide sequence. Moreover, TEV protease immobilized nanocomplexes conveniently removed and recollected from the reactant by applying an external magnetic field, maintained their enzymatic activity after reuse. Therefore, our newly developed nanoplatform for His-tagged enzyme immobilization provides advantageous features for biotechnological industries including recombinant protein processing.

ISSN 

0957-4484

Link 

http://dx.doi.org/10.1088/0957-4484/27/49/495705

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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