Hybrid nanoparticles based on organized protein immobilization on fullerenes.
Nanoscale carbon materials (i.e., fullerenes and nanotubes) are an attractive platform for applications in biotransformations and biosensors. The interesting properties displayed by nanoparticles demand new strategies for the manipulation of these materials on the nanoscale. Controlled modification of their surface with biomolecules is required to fully realize their potential in bionanotechnology. In this work, immobilization of a fullerene derivative with a mutant subtilisin is demonstrated, and the effect of the fullerene on the protein activity is determined. The fullerene-conjugated enzyme had improved catalytic properties in comparison to subtilisin immobilized on nonporous silica. Further, the pH profile of free and fullerene-conjugated subtilisin were almost identical.
Nednoor
Pramod
P
Department of Chemistry, University of Kentucky, Lexington, Kentucky 40506-0055, USA.
Capaccio
Marcello
M
Gavalas
Vasilis G
VG
Meier
Mark S
MS
Anthony
John E
JE
Bachas
Leonidas G
LG
D004800:Enzymes, Immobilized; D037741:Fullerenes / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D008863:Microspheres; D036103:Nanotechnology; D015202:Protein Engineering; D011506:Proteins / Q000737:chemistry*; D020860:Subtilisin / Q000737:chemistry*; D013499:Surface Properties
D004800:Enzymes, Immobilized; D037741:Fullerenes; D011506:Proteins; D020860:Subtilisin