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

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.

Key words： silica nanoparticles; biocatalysis; biomimetic synthesis; β-glucuronidase encapsulation; storage and recycling stability

Acknowledgments

The authors thank the financial support from the Specialized Research Fund for the Doctoral Program of Higher Education (20130032110023), National Science Foundation of China (21076145), the Program for New Century Excellent Talents in University (NCET-10-0623), the National Basic Research Program of China (2009CB724705), National Science Fund for Distinguished Young Scholars (21125627).

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