BROWSE

Related Researcher

Author's Photo

Kim, Byeong-Su
Soft and Hybrid Nanomaterials Lab
Research Interests
  • Carbon materials, polymer, Layer-by-Layer (LbL) assembly, hyperbranched polymer, polyglycerol (PG), bio-applications

ITEM VIEW & DOWNLOAD

Encapsulated magnetic nanoparticles as supports for proteins and recyclable biocatalysts

Cited 58 times inthomson ciCited 57 times inthomson ci
Title
Encapsulated magnetic nanoparticles as supports for proteins and recyclable biocatalysts
Author
Herdt, Aimee R.Kim, Byeong-SuTaton, T. Andrew
Keywords
HISTIDINE-TAGGED PROTEINS; GREEN FLUORESCENT PROTEIN; GOLD NANOPARTICLES; AFFINITY-CHROMATOGRAPHY; CELL-SURFACE; IMMOBILIZATION; ENZYMES; BINDING; COORDINATION; NANOSPHERES
Issue Date
2007-01
Publisher
AMER CHEMICAL SOC
Citation
BIOCONJUGATE CHEMISTRY, v.18, no.1, pp.183 - 189
Abstract
This paper describes the bioconjugation of histidine-tagged enzymes and other proteins to the surface of composite "magnetomicelles" consisting of magnetic γ-Fe2O3 nanoparticles encapsulated within cross-linked polystyrene-block-polyacrylate copolymer micelle shells. Free carboxylic acid groups on the magnetomicelle surface were converted to Cu2+-iminodiacetic acid (IDA) for protein capture. The conjugation of T4 DNA ligase and enhanced green fluorescent protein to magnetomicelles revealed that proteins were captured with a high surface density and could be magnetically separated from reaction mixtures and subsequently released from the nanoparticle surface. Additionally, bioconjugation of T7 RNA polymerase yielded a functional enzyme that maintained its biological activity and could be recycled for up to three subsequent transcription reactions. We propose that protein-magnetomicelle bioconjugates are effective for protein bioseparation and enzymatic recycling and further strengthen the idea that nanoparticle surfaces have utility in protein immobilization.
URI
Go to Link
DOI
10.1021/bc060215j
ISSN
1043-1802
Appears in Collections:
PHY_Journal Papers
Files in This Item:
2-s2.0-33846421601.pdf Download

find_unist can give you direct access to the published full text of this article. (UNISTARs only)

Show full item record

qrcode

  • mendeley

    citeulike

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

MENU