Silica-immobilized enzymes for multi-step synthesis in microfluidic devices

Authors

  • Heather R. Luckarift,

    1. Air Force Research Laboratory, 139 Barnes Drive, Tyndall AFB, Florida 32403
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  • Bosung S. Ku,

    1. Department of Chemical and Biological Engineering, Rensselaer Polytechnic Institute, Troy, New York 12180
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  • Jonathan S. Dordick,

    Corresponding author
    1. Department of Chemical and Biological Engineering, Rensselaer Polytechnic Institute, Troy, New York 12180
    • Department of Chemical and Biological Engineering, Rensselaer Polytechnic Institute, Troy, New York 12180; telephone: 518-276-2899; fax: 518-276-2207.
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  • Jim C. Spain

    Corresponding author
    1. School of Civil and Environmental Engineering, 311 Ferst Drive, Georgia Institute of Technology, Atlanta, Georgia 30332-051
    • School of Civil and Environmental Engineering, 311 Ferst Drive, Georgia Institute of Technology, Atlanta, Georgia 30332-051; telephone: 404-894-0628; fax: 404-894-2278.
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Abstract

The combinatorial synthesis of 2-aminophenoxazin-3-one (APO) in a microfluidic device is reported. Individual microfluidic chips containing metallic zinc, silica-immobilized hydroxylaminobenzene mutase and silica-immobilized soybean peroxidase are connected in series to create a chemo-enzymatic system for synthesis. Zinc catalyzes the initial reduction of nitrobenzene to hydroxylaminobenzene which undergoes a biocatalytic conversion to 2-aminophenol, followed by enzymatic polymerization to APO. Silica-immobilization of enzymes allows the rapid stabilization and integration of the biocatalyst within a microfluidic device with minimal preparation. The system proved suitable for synthesis of a complex natural product (APO) from a simple substrate (nitrobenzene) under continuous flow conditions. Biotechnol. Bioeng. 2007;98: 701–705. © 2007 Wiley Periodicals, Inc.

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