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Improvement of stability and reaction behavior of enzymes in organic solutions by immobilization onto nano-porous supports

Research Project

Project/Area Number 09555256
Research Category

Grant-in-Aid for Scientific Research (B)

Allocation TypeSingle-year Grants
Section展開研究
Research Field 生物・生体工学
Research InstitutionOkayama University

Principal Investigator

IMAMURA Koreyosi (1998)  OKAYAMA UNIV., ENGINEERING,ASSISTAN, 工学部, 助手 (70294436)

崎山 高明 (1997)  岡山大学, 工学部, 講師 (70170628)

Co-Investigator(Kenkyū-buntansha) UTAGAWA Takashi  AJINOMOTO CO., INC., Central Research Lab.CHIEF DIRECTOR, 生産技術部, 部長(研究職)
NAKANISHI Kazuhiro  OKAYAMA UNIV., ENGINEERING,PROFESSOR, 工学部, 教授 (90026584)
今村 維克  岡山大学, 工学部, 助手 (70294436)
Project Period (FY) 1997 – 1998
Project Status Completed (Fiscal Year 1998)
Budget Amount *help
¥1,100,000 (Direct Cost: ¥1,100,000)
Fiscal Year 1998: ¥1,100,000 (Direct Cost: ¥1,100,000)
Keywordsnon-aqueous enzymatic reaction / immobilized enzyme / thermolysin / satbility / peptide synthesis / aspartame / partition / 二相系反応 / 失活速度 / ペプチド合成 / 有機溶媒 / 熱安定性
Research Abstract

In this study, we intended to establish theoretical bases, which are required to realize enzymatic syntheses in organic solvents. We studied the synthetic reaction of aspartame precursor, Z-L-Asp-L-PheOMe, from respective amino acid derivatives (Z-Asp and PheOMe) catalyzed by thermolysin. First, we investigated various factors affecting stability of the immobilized thermolysin and analyzed its mechanism. Autolysis was found to be a main cause for inactivation in water-immiscible organic solvents and the immobilized enzyme tended to be inactivated in organic solvents with lower solubility of water. In particular, the immobilized was stable in tert-amyl alcohol probably because that aqueous phase around the enzyme immobilized is thin and as a result autolysis tended to be repressed. The method to predict the overall partition coefficient of the substrates containing acid and amine components was proposed, by taking into consideration the effect of ion-pair complexes formed between the substrates.
The synthetic rate with the immobilized enzyme in an organic solvent, containing a small amount of water could be in principle estimated on the basis of the model for the biphasic reaction when the amount of enzyme loaded was not so much. Namely, in the synthetic reactions, the both components of the substrate are partitioned into the water phase inside the support, and then converted to the product by the action of the enzyme, and finally the product is transferred into the bulk organic phase.

Report

(3 results)
  • 1998 Annual Research Report   Final Research Report Summary
  • 1997 Annual Research Report
  • Research Products

    (3 results)

All Other

All Publications (3 results)

  • [Publications] M.Miyanaga, et al.: "On the Stability of Immobilized Thermolysins in Organic Solvents" Journal of Bioscience and Bioengineering. (in press). (1999)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1998 Final Research Report Summary
  • [Publications] M.Miyanaga, et al.: "On the Stability of Immobilized Thermolysins in Organic Solvents." Journal of Bioscience and Bioengineering. (in press).

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1998 Final Research Report Summary
  • [Publications] M.Miyanaga,et al.: "On the Stability of Immobilized Thermolysins in Organic Solvents" Journal of Bioscience and Bioengineering. (in press). (1999)

    • Related Report
      1998 Annual Research Report

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Published: 1998-04-01   Modified: 2016-04-21  

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