Enzyme encapsulation using highly ordered mesoporous silica monoliths

Shun Ichi Matsuura*, Sherif A. El-Safty, Manami Chiba, Emiko Tomon, Tatsuo Tsunoda, Taka Aki Hanaoka

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    18 Citations (Scopus)


    Lipase encapsulation in 12 highly ordered mesoporous silica monoliths (HOMs) with different pore diameters (3-8 nm) and pore structures (2D and 3D mesostructures) was successfully achieved without leaching of the enzyme from the enzyme-HOM composite. The amount of lipase adsorbed on the HOMs was dependent on the pore diameter and pore structure. The 3D mesostructures had better enzyme adsorption capability than did the 2D mesostructures. Reaction kinetics showed that the lipase-HOM composites maintained high enzymatic activity during the hydrolysis of a triglyceride (80-85 of the activity of the free enzyme). Moreover, the thermal stability of the composites was greater than that of the free enzyme. These results strongly demonstrated the ability of HOM-n monoliths to act as supports for the stable immobilization of enzymes, with minimal loss of enzymatic activity.

    Original languageEnglish
    Pages (from-to)184-187
    Number of pages4
    JournalMaterials Letters
    Publication statusPublished - 2012 Dec 15


    • Enzyme activity
    • Enzyme encapsulation
    • Hydrolysis
    • Lipase
    • Mesoporous silica

    ASJC Scopus subject areas

    • General Materials Science
    • Condensed Matter Physics
    • Mechanical Engineering
    • Mechanics of Materials


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