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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dc.contributor.authorM K Shin-
dc.contributor.authorB Kang-
dc.contributor.authorNam Kyung Yoon-
dc.contributor.authorM H Kim-
dc.contributor.authorJ Ki-
dc.contributor.authorS Han-
dc.contributor.authorJungoh Ahn-
dc.contributor.authorS Haam-
dc.date.accessioned2017-04-19T10:29:09Z-
dc.date.available2017-04-19T10:29:09Z-
dc.date.issued2016-
dc.identifier.issn0957-4484-
dc.identifier.uri10.1088/0957-4484/27/49/495705ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/13501-
dc.description.abstractImmobilizing 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.-
dc.publisherIOP Publishing Ltd-
dc.titleSynthesis of Fe3O4@nickel-silicate core-shell nanoparticles for His-tagged enzyme immobilizing agents = 히시티딘 태그된 효소 고정화를 위한 코에셀 나노파티클 합성-
dc.title.alternativeSynthesis of Fe3O4@nickel-silicate core-shell nanoparticles for His-tagged enzyme immobilizing agents-
dc.typeArticle-
dc.citation.titleNanotechnology-
dc.citation.number49-
dc.citation.endPage495705-
dc.citation.startPage495705-
dc.citation.volume27-
dc.contributor.affiliatedAuthorNam Kyung Yoon-
dc.contributor.affiliatedAuthorJungoh Ahn-
dc.contributor.alternativeName신무광-
dc.contributor.alternativeName강병훈-
dc.contributor.alternativeName윤남경-
dc.contributor.alternativeName김명훈-
dc.contributor.alternativeName기지선-
dc.contributor.alternativeName한승민-
dc.contributor.alternativeName안정오-
dc.contributor.alternativeName함승주-
dc.identifier.bibliographicCitationNanotechnology, vol. 27, no. 49, pp. 495705-495705-
dc.identifier.doi10.1088/0957-4484/27/49/495705-
dc.subject.keywordcleavage-
dc.subject.keywordenzyme immobilization-
dc.subject.keywordHis-tag-
dc.subject.keywordnickel silicate covered superparamagnetic nanoparticle-
dc.subject.keywordTEV protease-
dc.subject.localcleavage-
dc.subject.localenzyme immobilization-
dc.subject.localEnzyme immobilization-
dc.subject.localHis-tag-
dc.subject.localnickel silicate covered superparamagnetic nanoparticle-
dc.subject.localTEV protease-
dc.description.journalClassY-
Appears in Collections:
Division of Bio Technology Innovation > BioProcess Engineering Center > 1. Journal Articles
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