Enzyme encapsulation using highly ordered mesoporous silica monoliths

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

    研究成果: Article

    14 引用 (Scopus)

    抄録

    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.

    元の言語English
    ページ(範囲)184-187
    ページ数4
    ジャーナルMaterials Letters
    89
    DOI
    出版物ステータスPublished - 2012 12 15

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    Encapsulation
    Silicon Dioxide
    enzymes
    Enzymes
    Silica
    silicon dioxide
    Lipases
    Lipase
    porosity
    Pore structure
    composite materials
    Composite materials
    leaching
    immobilization
    Catalyst supports
    Reaction kinetics
    Leaching
    hydrolysis
    Hydrolysis
    Triglycerides

    ASJC Scopus subject areas

    • Materials Science(all)
    • Condensed Matter Physics
    • Mechanical Engineering
    • Mechanics of Materials

    これを引用

    Matsuura, S. I., El-Safty, S. A., Chiba, M., Tomon, E., Tsunoda, T., & Hanaoka, T. A. (2012). Enzyme encapsulation using highly ordered mesoporous silica monoliths. Materials Letters, 89, 184-187. https://doi.org/10.1016/j.matlet.2012.08.110

    Enzyme encapsulation using highly ordered mesoporous silica monoliths. / Matsuura, Shun Ichi; El-Safty, Sherif A.; Chiba, Manami; Tomon, Emiko; Tsunoda, Tatsuo; Hanaoka, Taka Aki.

    :: Materials Letters, 巻 89, 15.12.2012, p. 184-187.

    研究成果: Article

    Matsuura, SI, El-Safty, SA, Chiba, M, Tomon, E, Tsunoda, T & Hanaoka, TA 2012, 'Enzyme encapsulation using highly ordered mesoporous silica monoliths', Materials Letters, 巻. 89, pp. 184-187. https://doi.org/10.1016/j.matlet.2012.08.110
    Matsuura SI, El-Safty SA, Chiba M, Tomon E, Tsunoda T, Hanaoka TA. Enzyme encapsulation using highly ordered mesoporous silica monoliths. Materials Letters. 2012 12 15;89:184-187. https://doi.org/10.1016/j.matlet.2012.08.110
    Matsuura, Shun Ichi ; El-Safty, Sherif A. ; Chiba, Manami ; Tomon, Emiko ; Tsunoda, Tatsuo ; Hanaoka, Taka Aki. / Enzyme encapsulation using highly ordered mesoporous silica monoliths. :: Materials Letters. 2012 ; 巻 89. pp. 184-187.
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    abstract = "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.",
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