Synthesis of Fe3O4@nickel-silicate core-shell nanoparticles for His-tagged enzyme immobilizing agents = 히시티딘 태그된 효소 고정화를 위한 코에셀 나노파티클 합성

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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
Author(s)
M K Shin; B Kang; Nam Kyung Yoon; M H Kim; J Ki; S Han; Jungoh Ahn; S Haam
Bibliographic Citation
Nanotechnology, vol. 27, no. 49, pp. 495705-495705
Publication Year
2016
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.
Keyword
cleavageenzyme immobilizationHis-tagnickel silicate covered superparamagnetic nanoparticleTEV protease
ISSN
0957-4484
Publisher
IOP Publishing Ltd
DOI
http://dx.doi.org/10.1088/0957-4484/27/49/495705
Type
Article
Appears in Collections:
Division of Bio Technology Innovation > BioProcess Engineering Center > 1. Journal Articles
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