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Crosslinked enzyme aggregates in hierarchically-ordered mesoporous silica: A simple and effective method for enzyme stabilization

Authors

  • Moon Il Kim,

    1. Department of Chemical and Biomolecular Engineering, Korea Advanced Institute of Science and Technology (KAIST), Daejeon 305-701, Republic of Korea; telephone: +82-42-869-3932; fax: +82-42-869-3910
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  • Jungbae Kim,

    1. Pacific Northwest National Laboratory, Richland, Washington 99352
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  • Jinwoo Lee,

    1. National Creative Research Initiative Center for Oxide Nanocrystalline Materials and School of Chemical Engineering, Seoul National University, Seoul, Republic of Korea
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  • Hongfei Jia,

    1. Department of Chemical Engineering, University of Akron, Akron, Ohio
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  • Hyon Bin Na,

    1. National Creative Research Initiative Center for Oxide Nanocrystalline Materials and School of Chemical Engineering, Seoul National University, Seoul, Republic of Korea
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  • Jong Kyu Youn,

    1. Department of Chemical and Biomolecular Engineering, Korea Advanced Institute of Science and Technology (KAIST), Daejeon 305-701, Republic of Korea; telephone: +82-42-869-3932; fax: +82-42-869-3910
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  • Ja Hun Kwak,

    1. Pacific Northwest National Laboratory, Richland, Washington 99352
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  • Alice Dohnalkova,

    1. Pacific Northwest National Laboratory, Richland, Washington 99352
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  • Jay W. Grate,

    1. Pacific Northwest National Laboratory, Richland, Washington 99352
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  • Ping Wang,

    1. Department of Chemical Engineering, University of Akron, Akron, Ohio
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  • Taeghwan Hyeon,

    1. National Creative Research Initiative Center for Oxide Nanocrystalline Materials and School of Chemical Engineering, Seoul National University, Seoul, Republic of Korea
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  • Hyun Gyu Park,

    Corresponding author
    1. Department of Chemical and Biomolecular Engineering, Korea Advanced Institute of Science and Technology (KAIST), Daejeon 305-701, Republic of Korea; telephone: +82-42-869-3932; fax: +82-42-869-3910
    • Department of Chemical and Biomolecular Engineering, Korea Advanced Institute of Science and Technology (KAIST), Daejeon 305-701, Republic of Korea; telephone: +82-42-869-3932; fax: +82-42-869-3910.
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  • Ho Nam Chang

    1. Department of Chemical and Biomolecular Engineering, Korea Advanced Institute of Science and Technology (KAIST), Daejeon 305-701, Republic of Korea; telephone: +82-42-869-3932; fax: +82-42-869-3910
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Abstract

α-chymotrypsin (CT) and lipase (LP) were immobilized in hierarchically-ordered mesocellular mesoporous silica (HMMS) in a simple but effective way for the enzyme stabilization, which was achieved by the enzyme adsorption followed by glutaraldehyde (GA) crosslinking. This resulted in the formation of nanometer scale crosslinked enzyme aggregates (CLEAs) entrapped in the mesocellular pores of HMMS (37 nm), which did not leach out of HMMS through narrow mesoporous channels (13 nm). CLEA of α-chymotrypsin (CLEA-CT) in HMMS showed a high enzyme loading capacity and significantly increased enzyme stability. No activity decrease of CLEA-CT was observed for 2 weeks under even rigorously shaking condition, while adsorbed CT in HMMS and free CT showed a rapid inactivation due to the enzyme leaching and presumably autolysis, respectively. With the CLEA-CT in HMMS, however, there was no tryptic digestion observed suggesting that the CLEA-CT is not susceptible to autolysis. Moreover, CLEA of lipase (CLEA-LP) in HMMS retained 30% specific activity of free lipase with greatly enhanced stability. This work demonstrates that HMMS can be efficiently employed as host materials for enzyme immobilization leading to highly enhanced stability of the immobilized enzymes with high enzyme loading and activity. Biotechnol. Bioeng. 2007;96: 210–218. © 2006 Wiley Periodicals, Inc.

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