Amphiphilic network as nanoreactor for enzymes in organic solvents.
Enzymes are powerful biocatalysts that work naturally in water but are also active in organic solvents. Here, we present a nanophase-separated amphiphilic network, where an enzyme is entrapped into its hydrophilic domains. A substrate that diffuses into the other, hydrophobic, phase of such a network can access the biocatalyst via the extremely large interface. Entrapped horseradish peroxidase and chloroperoxidase showed dramatically increased activity and operational stability compared to the native enzymes.
Bruns
Nico
N
Freiburg Materials Research Center (FMF) and Institute of Macromolecular Chemistry, Albert-Ludwigs-University Freiburg, Stefan-Meier-Strasse 21, 79104 Freiburg, Germany.
Tiller
Joerg C
JC
D002384:Catalysis; D002711:Chloride Peroxidase / Q000737:chemistry*; D004129:Dimethylpolysiloxanes / Q000737:chemistry*; D004795:Enzyme Stability; D004800:Enzymes, Immobilized; D006735:Horseradish Peroxidase / Q000737:chemistry*; D018625:Microscopy, Atomic Force; D036103:Nanotechnology; D011102:Polyhydroxyethyl Methacrylate / Q000031:analogs & derivatives* / Q000737:chemistry; D012997:Solvents; D013501:Surface-Active Agents / Q000737:chemistry*; D014867:Water
D004129:Dimethylpolysiloxanes; D004800:Enzymes, Immobilized; D012997:Solvents; D013501:Surface-Active Agents; D014867:Water; D011102:Polyhydroxyethyl Methacrylate; C023037:poly(2-hydroxyethyl acrylate); D006735:Horseradish Peroxidase; D002711:Chloride Peroxidase