Enzyme immobilization on gold/Fe-oxide composite nanoparticles using a methionine tag

Autor:	Yuichi Koga, Michika Abe, Takashi Nakagawa, Kazuma Watanabe, Takao A. Yamamoto, Toshihiro Shikakura, Satoshi Seino
Rok vydání:	2014
Předmět:	chemistry.chemical_classification Methionine Immobilized enzyme biology Iron oxide Nanoparticle Enzyme assay chemistry.chemical_compound Colloid and Surface Chemistry Enzyme chemistry biology.protein Organic chemistry Specific activity Nanocarriers Nuclear chemistry
Zdroj:	Colloids and Surfaces A: Physicochemical and Engineering Aspects. 459:298-301
ISSN:	0927-7757
DOI:	10.1016/j.colsurfa.2014.06.049
Popis:	We developed a novel technique for immobilizing enzymes on magnetic nanoparticle surfaces by using a methionine-tag system. Au/Fe-oxide composite nanoparticles synthesized through a radiochemical process were used as magnetic nanocarriers. The C-terminus of Tk-subtilisin, a model enzyme, was modified with a methionine tag and mixed with Au/Fe-oxide composite nanoparticles for immobilization via Au-S bonding. Methionine-tagged immobilized enzymes showed 98% residual specific activity, while the untagged enzymes showed 78%. The methionine-tagged immobilized enzymes retained their activities in a wide temperature range of 30–70 °C. Thus, the methionine-tag system provided orientational immobilization via the formation of Au-S bonds, which resulted in structural stability of the immobilized enzymes.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::c85ed5c20cb891a419ccbb41cb2bf81e https://doi.org/10.1016/j.colsurfa.2014.06.049 Zobrazit plný text záznamu Full Text from ScienceDirect