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A Magnetically Separable, Highly Stable Enzyme System Based on Nanocomposites of Enzymes and Magnetic Nanoparticles Shipped in Hierarchically Ordered, Mesocellular, Mesoporous Silica

Authors

  • Jungbae Kim Dr.,

    1. Pacific Northwest National Laboratory, Richland, WA 99352, USA, Fax: (+1) 509-376-5106
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  • Jinwoo Lee Dr.,

    1. National Creative Research Initiative Center for Oxide, Nanocrystalline Materials and School of Chemical and Biological Engineering, Seoul National University, Seoul, 151-744, Korea, Fax: (+82) 2-886-8457
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  • Hyon Bin Na,

    1. National Creative Research Initiative Center for Oxide, Nanocrystalline Materials and School of Chemical and Biological Engineering, Seoul National University, Seoul, 151-744, Korea, Fax: (+82) 2-886-8457
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  • Byoung Chan Kim Dr.,

    1. Advanced Environmental Monitoring Research Center, Gwangju Institute of Science and Technology, Gwangju, 500-712, Korea
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  • Jong Kyu Youn,

    1. Department of Chemical and Biomolecular Engineering, Korean Advanced Institute of Science and Technology, Daejeon, 350-701, Korea
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  • Ja Hun Kwak Dr.,

    1. Pacific Northwest National Laboratory, Richland, WA 99352, USA, Fax: (+1) 509-376-5106
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  • Karam Moon,

    1. Pacific Northwest National Laboratory, Richland, WA 99352, USA, Fax: (+1) 509-376-5106
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  • Eunwoong Lee,

    1. National Creative Research Initiative Center for Oxide, Nanocrystalline Materials and School of Chemical and Biological Engineering, Seoul National University, Seoul, 151-744, Korea, Fax: (+82) 2-886-8457
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  • Jaeyun Kim,

    1. National Creative Research Initiative Center for Oxide, Nanocrystalline Materials and School of Chemical and Biological Engineering, Seoul National University, Seoul, 151-744, Korea, Fax: (+82) 2-886-8457
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  • Jongnam Park Dr.,

    1. National Creative Research Initiative Center for Oxide, Nanocrystalline Materials and School of Chemical and Biological Engineering, Seoul National University, Seoul, 151-744, Korea, Fax: (+82) 2-886-8457
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  • Alice Dohnalkova,

    1. Pacific Northwest National Laboratory, Richland, WA 99352, USA, Fax: (+1) 509-376-5106
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  • Hyun Gyu Park Prof.,

    1. Department of Chemical and Biomolecular Engineering, Korean Advanced Institute of Science and Technology, Daejeon, 350-701, Korea
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  • Man Bock Gu Prof.,

    1. Graduate School of Biotechnology, Korea University, Seoul, 136-701, Korea
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  • Ho Nam Chang Prof.,

    1. Department of Chemical and Biomolecular Engineering, Korean Advanced Institute of Science and Technology, Daejeon, 350-701, Korea
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  • Jay W. Grate Dr.,

    1. Pacific Northwest National Laboratory, Richland, WA 99352, USA, Fax: (+1) 509-376-5106
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  • Taeghwan Hyeon Prof.

    1. National Creative Research Initiative Center for Oxide, Nanocrystalline Materials and School of Chemical and Biological Engineering, Seoul National University, Seoul, 151-744, Korea, Fax: (+82) 2-886-8457
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  • J.K. would like to thank the U.S. Department of Energy (DOE) LDRD funds administered by the Pacific Northwest National Laboratory, DARPA/MTO under Contract DE-AC05-76 L01830, and the DOE Office of Biological and Environmental Research under the Environmental Management Science Program. T.H. would like to thank the Korean Ministry of Science and Technology for financial support through the National Creative Research Initiative Program. The research was performed in part at the W. R. Wiley Environmental Molecular Sciences Laboratory, a national scientific user facility sponsored by the DOE’s Office of Biological and Environmental Research and located at the Pacific Northwest National Laboratory.

Abstract

original image

Multifunctional nanocomposites (M-CLEAs) of enzymes and magnetic nanoparticles (M-NPs) were fabricated in hierarchically ordered, mesocellular, mesoporous silica (HMMS; see Figure) by a simple process involving the co-adsorption of enzyme molecules and magnetic nanoparticles into HMMS followed by glutaraldehyde (GA) treatment. These nanocomposites are magnetically separable and highly stable and active. In particular, M-CLEA–lipase shows no decrease of lipase activity at all in the presence of proteases.

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