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Immobilization of β-glucuronidase in lysozyme-induced biosilica particles to improve its stability

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Abstract

Mesoporous silica particles were prepared for efficient immobilization of the β-glucuronidase (GUS) through a biomimetic mineralization process, in which the solution containing lysozyme and GUS were added into the prehydrolyzed tetraethoxysilane (TEOS) solution. The silica particles were formed in a way of biomineralization under the catalysis of lysozyme and GUS was immobilized into the silica particles simultaneously during the precipitation process. The average diameter of the silica particles is about 200 nm with a pore size of about 4 nm. All the enzyme molecules are tightly entrapped inside the biosilica nanoparticles without any leaching even under a high ionic strength condition. The immobilized GUS exhibits significantly higher thermal and pH stability as well as the storage and recycling stability compared with GUS in free form. No loss in the enzyme activity of the immobilized GUS was found after 30-day’s storage, and the initial activity could be well retained after 12 repeated cycles.

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Authors and Affiliations

  1. Key Laboratory for Green Chemical Technology of Ministry of Education, School of Chemical Engineering and Technology, Tianjin University, Tianjin, 300072, China

    Xiaokai Song, Zhongyi Jiang, Lin Li & Hong Wu

  2. Collaborative Innovation Center of Chemical Science and Engineering (Tianjin), Tianjin, 300072, China

    Zhongyi Jiang & Hong Wu

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  1. Xiaokai Song
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  2. Zhongyi Jiang
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  3. Lin Li
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  4. Hong Wu
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Correspondence to Hong Wu.

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Song, X., Jiang, Z., Li, L. et al. Immobilization of β-glucuronidase in lysozyme-induced biosilica particles to improve its stability. Front. Chem. Sci. Eng. 8, 353–361 (2014). https://doi.org/10.1007/s11705-014-1421-2

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  • DOI: https://doi.org/10.1007/s11705-014-1421-2

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