Characteristics of Hydrolysis with Lipase Immobilized in Mesoporous Silica

DOI Web Site Web Site 18 References
  • Maeda Satomi
    Department of Chemical Engineering, Faculty of Engineering, Kansai University
  • Choshi Kenichi
    Department of Chemical Engineering, Faculty of Engineering, Kansai University
  • Miyake Yoshikazu
    Department of Chemical Engineering, Faculty of Engineering, Kansai University High Technology Research Center, Kansai University

Bibliographic Information

Other Title
  • メソポーラスシリカ粒子に固定化したリパーゼによる加水分解反応特性
  • メソポーラスシリカ リュウシ ニ コテイカ シタ リパーゼ ニ ヨル カスイ ブンカイ ハンノウ トクセイ

Search this article

Abstract

Mesoporous silica powder (SBA15) with hexagonal pore structure (pore diameter, 7.5 nm and specific surface area, 584 m2/g) was prepared in the presence of tri-block copolymer as a template. Commercial mesoporous silica MCM41 with hexagonal pore structure (pore diameter, 2.9 nm and specific surface area, 759 m2/g) and SBA15 were used as a carrier for immobilization of a hydrolytic enzyme, lipase. SBA15 immobilized a greater amount of enzyme than MCM41 because of its larger pore diameter.<br>The hydrolysis of 2-naphthyl acetate with the lipase immobilized in mesoporous silica was examined at 25, 50 and 70°C by measuring the concentration of hydrolysis product, 2-naphthol. At 50 and 75°C, the immobilized lipase converted a greater proportion of 2-naphthyl acetate than the lipase in aqueous phase, and the conversion with MCM41 as carrier was greater than that with SBA15. On reuse of the immobilized lipase a conversion of more than 70% was obtained at 50°C. The thermal stability of lipase for the hydrolysis of 2-naphthyl acetate was increased by the immobilization of lipase in mesoporous silica.

Journal

References(18)*help

See more

Related Projects

See more

Keywords

Details 詳細情報について

Report a problem

Back to top