Encapsulated magnetic nanoparticles as supports for proteins and recyclable biocatalysts
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- Encapsulated magnetic nanoparticles as supports for proteins and recyclable biocatalysts
- Herdt, Aimee R.; Kim, Byeong-Su; Taton, T. Andrew
- HISTIDINE-TAGGED PROTEINS; GREEN FLUORESCENT PROTEIN; GOLD NANOPARTICLES; AFFINITY-CHROMATOGRAPHY; CELL-SURFACE; IMMOBILIZATION; ENZYMES; BINDING; COORDINATION; NANOSPHERES
- Issue Date
- AMER CHEMICAL SOC
- BIOCONJUGATE CHEMISTRY, v.18, no.1, pp.183 - 189
- 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.
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