Amphiphilic Network as Nanoreactor for Enzymes in Organic Solvents

• Published in: Nano letters Vol. 5; no. 1; pp. 45 - 48
• Main Authors: Bruns, Nico, Tiller, Joerg C
• Format: Journal Article
• Language: English
• Published: Washington, DC American Chemical Society 01-01-2005
• Subjects: Analytical biochemistry: general aspects, technics, instrumentation; Analytical, structural and metabolic biochemistry; Biological and medical sciences; Catalysis; Chemistry; Chloride Peroxidase - chemistry; Dimethylpolysiloxanes - chemistry; Electrochemistry; Electrodes: preparations and properties; Electrophoresis; Enzyme Stability; Enzymes, Immobilized; Exact sciences and technology; Fundamental and applied biological sciences. Psychology; General and physical chemistry; Horseradish Peroxidase - chemistry; Microscopy, Atomic Force; Nanotechnology; Polyhydroxyethyl Methacrylate - analogs & derivatives; Polyhydroxyethyl Methacrylate - chemistry; Solvents; Surface-Active Agents - chemistry; Water; Trapping; Biocatalysis; Peroxidases; Enzyme; Nanostructure; Peroxidase; Oxidoreductases; Diffusion; Experimental study; Chemical synthesis; Interface; Organic compounds
• ISSN: 1530-6984; 1530-6992
• DOI: 10.1021/nl048413b

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.