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Enzyme Entrapped in Polymer-Modified Nanopores: The Effects of Macromolecular Crowding and Surface Hydrophobicity

Authors

  • Jia Liu,

    1. State Key Laboratory of Catalysis, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, 457 Zhongshan Road, Dalian 116023 (China), Fax: (+86) 411-84694447
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  • Juan Peng,

    1. State Key Laboratory of Catalysis, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, 457 Zhongshan Road, Dalian 116023 (China), Fax: (+86) 411-84694447
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  • Shuai Shen,

    1. State Key Laboratory of Catalysis, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, 457 Zhongshan Road, Dalian 116023 (China), Fax: (+86) 411-84694447
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  • Qianru Jin,

    1. State Key Laboratory of Catalysis, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, 457 Zhongshan Road, Dalian 116023 (China), Fax: (+86) 411-84694447
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  • Prof. Dr. Can Li,

    Corresponding author
    1. State Key Laboratory of Catalysis, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, 457 Zhongshan Road, Dalian 116023 (China), Fax: (+86) 411-84694447
    • State Key Laboratory of Catalysis, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, 457 Zhongshan Road, Dalian 116023 (China), Fax: (+86) 411-84694447
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  • Prof. Dr. Qihua Yang

    Corresponding author
    1. State Key Laboratory of Catalysis, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, 457 Zhongshan Road, Dalian 116023 (China), Fax: (+86) 411-84694447
    • State Key Laboratory of Catalysis, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, 457 Zhongshan Road, Dalian 116023 (China), Fax: (+86) 411-84694447
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Abstract

Macromolecular crowding is an ubiquitous phenomenon in living cells that significantly affects the function of enzymes in vivo. However, this effect has not been paid much attention in the research of the immobilization of enzymes onto mesoporous silica. Herein, we report the combined effects of macromolecular crowding and surface hydrophobicity on the performance of an immobilized enzyme by accommodating lipase molecules into a series of mesoporous silicas with different amounts of inert poly(methacrylate) (PMA) covalently anchored inside the nanopores. The incorporation of the PMA polymer into the nanopores of mesoporous silica enables the fabrication of a crowded and hydrophobic microenvironment for the immobilized enzyme and the variation in polymer content facilitates an adjustment of the degree of crowding and surface properties of this environment. Based on this system, the catalytic features of immobilized lipase were investigated as a function of polymer content in nanopores and the results indicated that the catalytic efficiency, thermostability, and reusability of immobilized lipase could all be improved by taking advantage of the macromolecular crowding effect and surface hydrophobicity. These findings provide insight into the possible functions of the macromolecular crowding effect, which should be considered and integrated into the fabrication of suitable mesoporous silicas to improve enzyme immobilization.

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