• Search Research Projects
  • Search Researchers
  • How to Use
  1. Back to previous page

A study on biocatalysts immobilized in nanospace

Research Project

Project/Area Number 13650839
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field 触媒・化学プロセス
Research InstitutionThe University of Tokyo

Principal Investigator

ONAKA Makoto  The University of Tokyo, Graduate School of Arts and Sciences, Associate Professor, 大学院・総合文化研究科, 助教授 (10144122)

Project Period (FY) 2001 – 2002
Project Status Completed (Fiscal Year 2002)
Budget Amount *help
¥3,600,000 (Direct Cost: ¥3,600,000)
Fiscal Year 2002: ¥1,700,000 (Direct Cost: ¥1,700,000)
Fiscal Year 2001: ¥1,900,000 (Direct Cost: ¥1,900,000)
KeywordsMesoporous silica / Enzyme lipase / Immobilized enzyme / Biocatalyst system / Green chemical process / Sol-gel process / Long-chain carboxylic acid / Esterification / グリーンケミストリー / 生体触媒 / メソ多孔体シリカ
Research Abstract

The objectives of the research are to prepare stable biocatalyst systems encapsulated in nanoporous, hydrophobic space and to apply them to green-chemical organic synthesis in organic media. As a nanoporous material, we chose highly-ordered mesoporous silica with a pore size of 6-9 nanometer in diameter, which was prepared using Si(OEt)_4, and triblockcopolymer. The internal surface of the mesoporous silica was then modified by silane coupling agents having amino, hydroxyl, and carboxylic functional groups. Lipase enzyme was immobilized in the chemically-modified mesoporous silicas, and applied to esterification between an equimolar amount of carboxylic acid and alcohol under ambient conditions. We compared biocatalysis between lipase encapsulated in the chemically modified mesoporous silicas and commercially available lipase supported on Celite. We found several advantages: 1) Our lipase system showed 20 times as high biocatalysis in esterification as the conventional lipase, 2) the volume of our immobilized lipase is much smaller than that of Celite-supported lipase, 3) the stability of the lipase in mesoporous silica is much superior, and 4) no leaching of lipase from the pores of chemically-modified mesoporous silica was observed.

Report

(3 results)
  • 2002 Annual Research Report   Final Research Report Summary
  • 2001 Annual Research Report
  • Research Products

    (4 results)

All Other

All Publications (4 results)

  • [Publications] T.Itoh, N.Ouchi, Y.Nishimura, H.S.Hui, N.Katada, M.Niwa, M.Onaka: "Novel Supporting Materials of Lipase PS Suitable for Use in an Ionic Liquid Solvent System"Green Chemistry. 5. 494-496 (2003)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2002 Final Research Report Summary
  • [Publications] T.Itoh, Y.Nishimura, M.kashiwagi, M.Onaka: "Efficient Lipase-catalyzed Enantioselective Acylation in an Ionic Liquid Solvent System"Ionic Liquids as Green Solvents : Progress and Prospects, ACS Symposium Series. 856. 251-261 (2003)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2002 Final Research Report Summary
  • [Publications] T.Itoh, N.Ouchi, Y.Nishimura, H.S.Hui, N.Katada, M.Niwa, M.Onaka: "Novel Supporting Materials of Lipase PS Suitable for Use in an Ionic Liquid Solvent System"Green Chemistry. 5. 494-496 (2003)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2002 Final Research Report Summary
  • [Publications] T.Itoh, Y.Nishimura, M.Kashiwagi, M.Onaka: "Efficient Lipase-catalyzed Enantioselective Acylation in an Ionic Liquid Solvent Syste"Ionic.Liquids as Green Solvents ; Progress and Prospects, ACS Symposium Series 856. 251-261 (2003)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2002 Final Research Report Summary

URL: 

Published: 2001-04-01   Modified: 2016-04-21  

Information User Guide FAQ News Terms of Use Attribution of KAKENHI

Powered by NII kakenhi