Enzymatic self-sacrificial display of an active protein on gold nanoparticles

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

A new enzymatic approach for the fabrication of gold nanoparticles (Au NPs) decorated with a functional protein was developed using a recombinant glycerol dehydrogenase from Bacillus stearothermophilus (BsGLD) that was tagged with an N-terminal protein G domain and a C-terminal (His)6Cys tag. The recombinant BsGLD promoted the synthesis of the Au NPs via the catalytic reduction of nicotinamide adenine dinucleotide using glycerol as a substrate, and the recombinant BsGLD was self-immobilized on the Au NPs as a result of the protein G's binding capability for IgG antibody.

Original languageEnglish
Pages (from-to)5995-5998
Number of pages4
JournalRSC Advances
Volume4
Issue number12
DOIs
Publication statusPublished - Jan 17 2014

Fingerprint

glycerol dehydrogenase
Glycerol
Gold
Display devices
Nanoparticles
Proteins
Bacilli
Antibodies
NAD
Immunoglobulin G
Fabrication
Substrates
Protein Binding
Oxidoreductases

All Science Journal Classification (ASJC) codes

  • Chemical Engineering(all)
  • Chemistry(all)

Cite this

Enzymatic self-sacrificial display of an active protein on gold nanoparticles. / Niide, Teppei; Goto, Masahiro; Kamiya, Noriho.

In: RSC Advances, Vol. 4, No. 12, 17.01.2014, p. 5995-5998.

Research output: Contribution to journalArticle

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