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Related Concept Videos

Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

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The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at high-speed. Their catalytic efficiency values range from 108-109 M-1s-1. These enzymes are also called 'diffusion-controlled' as the only rate-limiting step in the catalysis is that of the substrate diffusion into the active site. Examples include triose phosphate isomerase, fumarase, and superoxide dismutase.
 
Most enzymes...
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Related Experiment Video

Updated: Jul 27, 2025

Immobilization of Multi-biocatalysts in Alginate Beads for Cofactor Regeneration and Improved Reusability
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Highly efficient and recyclable monolithic bioreactor for interfacial enzyme catalysis.

Zhengqiao Yin1, Yiding Zhou1, Xiucai Liu1

  • 1Shanghai Key Laboratory of Advanced Polymeric Materials, Key Laboratory for Ultrafine Materials of Ministry of Education, School of Materials Science and Engineering, East China University of Science and Technology, Shanghai 200237, China.

Journal of Colloid and Interface Science
|June 10, 2023
PubMed
Summary

A novel microreactor system effectively immobilizes enzymes using polymersomes within porous monoliths. This biocatalysis approach ensures high enzyme reusability and product purity in repeated batch reactions.

Keywords:
Biphasic biocatalystEmulsion-templateMonolithic bioreactorPickering emulsionPolymersome

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Area of Science:

  • Biocatalysis and Enzyme Engineering
  • Materials Science and Engineering
  • Chemical Engineering

Background:

  • Biocatalysts are essential for bioconversions but integrating them with substrates in artificial systems is challenging.
  • Existing methods like Pickering interfacial catalysis and microchannel reactors have limitations in efficiency and reusability.
  • An effective, reusable monolith system for combining chemical substrates and biocatalysts is still needed.

Purpose of the Study:

  • To develop a novel, highly efficient, and reusable microreactor system for biphasic interfacial biocatalysis.
  • To create a monolith system capable of integrating chemical substrates and biocatalysts effectively.
  • To overcome the limitations of current artificial reaction systems involving biocatalysts.

Main Methods:

  • Developed a repeated batch-type biphasic interfacial biocatalysis microreactor.
  • Utilized enzyme-loaded polymersomes (Candida antarctica Lipase B - CALB) within the pores of porous monoliths.
  • Fabricated polymersomes via self-assembly of PEO-b-P(St-co-TMI) and used them to stabilize oil-in-water Pickering emulsions as templates for monolith preparation.

Main Results:

  • The microreactor demonstrated high effectiveness and recyclability in substrate processing.
  • Achieved absolute product purity with no enzyme loss across multiple cycles.
  • Maintained over 93% relative enzyme activity across 15 cycles.
  • Ensured enzyme stability and immunity to inactivation within the microenvironment.

Conclusions:

  • The developed microreactor system offers a highly efficient and reusable solution for biocatalysis.
  • The system provides superior product separation and enzyme retention capabilities.
  • This approach facilitates enzyme recycling and maintains high activity over extended use.