Related Experiment Video
Updated: Jul 3, 2026

Development of Heterogeneous Enantioselective Catalysts using Chiral Metal-Organic Frameworks (MOFs)
Published on: January 17, 2020
New formulae for folding catalysts make them multi-purpose enzymes
M Moutiez1, R Guthapfel, P Gueguen
1CEA, Département d'Ingénierie et d'Etudes des Protéines, Bâtiment 152, C.E. Saclay, F-91191 Gif-sur-Yvette, France; telephone: (33)1-69.08.76.48; fax: (33)1-69.08.90.71.
Immobilizing protein disulfide isomerase (PDI) and prolyl isomerase (PPI) on agarose beads overcomes limitations for large-scale protein folding. Modified enzymes enhance efficiency and enable new biochemical reactor designs.
Area of Science:
- Biotechnology
- Enzyme Engineering
- Biocatalysis
Background:
- Protein disulfide isomerase (PDI) and prolyl isomerase (PPI) are effective protein folding catalysts.
- Large-scale applications are limited by economic and technical challenges.
Purpose of the Study:
- To immobilize PDI and PPI on cross-linked agarose beads.
- To overcome enzyme inactivation during immobilization and maintain catalytic activity.
- To explore applications in biochemical reactors and other processes.
Main Methods:
- Immobilization of PDI and PPI onto cross-linked agarose beads.
- Oxidation of active site thiols with dimethylsulfoxide to prevent PDI inactivation.
- Biotinylation of PDI and PPI to enhance stability and activity.
Main Results:
- Successfully immobilized PDI and PPI with retained activity.
- Achieved 64% activity for PDI immobilized via thiol oxidation.
- Obtained 100% activity for PPI and 55-66% for PDI after biotinylation.
- Demonstrated suppression of post-refolding purification requirements.
Conclusions:
- Immobilized PDI and PPI offer a viable solution for large-scale protein folding.
- Enzyme modification strategies (thiol oxidation, biotinylation) are effective in preserving activity.
- This approach facilitates the development of efficient biochemical reactors and novel applications.
More Related Videos
09:27Immobilization of Multi-biocatalysts in Alginate Beads for Cofactor Regeneration and Improved Reusability
Published on: April 22, 2016
12:08Catalytic Reactions at Amine-Stabilized and Ligand-Free Platinum Nanoparticles Supported on Titania During Hydrogenation of Alkenes and Aldehydes
Published on: June 24, 2022
Related Concept Videos
Introduction to Mechanisms of Enzyme Catalysis
Introduction to Mechanisms of Enzyme Catalysis
Heterogeneous Catalysis
Enzymes
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
Catalytically Perfect Enzymes
Induced-fit Model
Enzymes exhibit substrate specificity, meaning that they can only bind to certain substrates. This is mainly determined by the shape and chemical characteristics of...