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Two-phase system membrane reactor with cofactor recycling.

S Kise1, M Hayashida

  • 1Department of Bioscience Research Center, Mitsui Petrochemical Industries, Ltd., Yamaguchi, Japan.

Journal of Biotechnology
|May 1, 1990
PubMed
Summary
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Enzyme immobilization enhanced menthone reductase stability for efficient l-menthol production. A novel reactor design enabled continuous synthesis with cofactor recycling, achieving high product yield and enzyme longevity.

Area of Science:

  • Biocatalysis and enzyme engineering
  • Chemical reaction engineering
  • Bioprocess development

Background:

  • Enzymatic synthesis offers sustainable routes for valuable chemicals like l-menthol.
  • Cofactor dependency and enzyme stability are key challenges in biocatalytic processes.
  • Efficient reactor design is crucial for continuous bioproduction and economic viability.

Purpose of the Study:

  • To investigate the enzymatic production of l-menthol using a model two-phase system reactor.
  • To enhance enzyme stability and activity through immobilization.
  • To achieve continuous l-menthol production with effective cofactor recycling.

Main Methods:

  • Immobilization of menthone reductase onto activated carbon.
  • Utilizing methyl isobutyl carbinol as a co-substrate for NADH regeneration.

Related Experiment Videos

  • Development of a two-phase reactor system with a hydrophobic microfiltration membrane for product separation and cofactor/enzyme retention.

    • Main Results:

    • Immobilized menthone reductase exhibited a four-fold longer half-life compared to the free enzyme.
    • Continuous l-menthol production was sustained for over 270 hours at a rate of 46.1 g/L/day.
    • High cofactor recycling numbers (up to 3020) and efficient separation of l-menthol were achieved.

    Conclusions:

    • Enzyme immobilization significantly improves biocatalyst stability and process efficiency.
    • The developed reactor system facilitates continuous l-menthol production with effective cofactor and enzyme retention.
    • This approach demonstrates a viable strategy for the industrial-scale enzymatic synthesis of chiral compounds.