Fabrication, characterization, and enzymatic activity of fungal protease--nanogold membrane bioconjugate.
This study describes the synthesis of a free-standing nanogold membrane by the spontaneous reduction of aqueous chloroaurate ions by the diamine molecule DAEE at a liquid-liquid interface. The free standing nanogold membrane, provides a biocompatible surface for the immobilization of proteins. F-Protease (F-Prot) was then bound to the nanogold membrane via interaction with the gold nanoparticles leading to a new class of biocatalyst. A highlight of the new biocatalyst wherein the enzyme is bound to the nanogold membrane is the ease with which separation from the reaction medium may be achieved by simple filtration. In relation to the free enzyme in solution, the F-Prot in the bioconjugate material exhibited a slightly higher biocatalytic activity and significantly enhanced pH and temperature stability. The F-Prot nanogold membrane bioconjugate material also exhibited excellent biocatalytic activity over ten successive reuse cycles.
Vinod
V P
VP
Biochemical Sciences Division, National Chemical Laboratory, Pune 411008, India.
Phadtare
S
S
Joshi
H M
HM
Sastry
Murali
M
Rao
Mala
M
D002384:Catalysis; D002713:Chlorine / Q000737:chemistry; D005656:Fungal Proteins / Q000737:chemistry*; D006046:Gold / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D007477:Ions; D053768:Metal Nanoparticles / Q000737:chemistry*; D046529:Microscopy, Electron, Transmission; D053761:Nanocomposites / Q000737:chemistry*; D053758:Nanoparticles / Q000737:chemistry; D036103:Nanotechnology / Q000379:methods; D010447:Peptide Hydrolases / Q000737:chemistry*; D013696:Temperature
D005656:Fungal Proteins; D007477:Ions; D002713:Chlorine; D006046:Gold; D010447:Peptide Hydrolases