Perpustakaan Digital ITB

In the present study, a novel bioinorganic catalytic interface,combining the in situ radical polymerization technique with the noncovalentadsorption method, was successfully fabricated, and its assembly mechanism wasexplored. The in situ radical polymerization technique was applied to construct apolymer shell around the enzyme surface to form the protein nanocapsule. Then,protein nanocapsules assembled on the surface of graphene oxide (GO) throughnoncovalent interactions to fabricate the dual-immobilized enzyme system. Here,native organophosphorus hydrolase (OPH) and OPH nanocapsule (nOPH10)were immobilized on GO to form the traditional immobilized OPH (OPH@GO)and dual-immobilized OPH (nOPH10@GO), respectively. The introducedpolymer shell could protect the enzyme from various denaturation factors andprovide abundant functional groups to interact with supports to strengthen theinteractions between them. Compared to native OPH and OPH@GO, theresulting nOPH10@GO exhibited enhanced catalytic activity, stability, and reusability. The nOPH10@GO was further used toconstruct the biosensor, which exhibited better detection performance compared with that of OPH@GO. These featuresindicated that the introduced enzyme immobilization system could enhance the enzymatic performance and broaden itsapplication prospect.