Immobilization of Enzymes Using Water-Soluble Metal-Organic Polyhedra

Immobilization of enzymes is a potent strategy to improve their applicability for industrial or technological applications. This highlight describes our strategy of developing a family of cage-like compounds called metal-organic polyhedra (MOPs) functionalized to have a high solubility in water, in order to form self-assembled structures with enzymes. The high affinity of the developed MOPs for the surface of proteins enabled an easy yet versatile “Mix-and-shake” method to form aggregates in which enzymes are cross-linked by robust microporous units. Furthermore, the physical state of the MOP-enzymes composites, from colloids to solid precipitates, can easily be controlled by adjusting the mixing MOP-to-protein ratio. Immobilized enzymes maintained a high catalytic activity in the solid-state, and also showed a good recyclability and an improved stability. Furthermore, the unique nature of MOPs as well-defined yet highly tunable nanosized molecular entities can be used to mimic microscale environments in complex systems, and modify proteins’ configuration and activity in well-controlled conditions.

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Publication Details

Journal
Kobunshi
Published
2024-12-31
DOI
https://doi.org/10.1295/kobunshi.74.1_15
Primary Topic
Diatoms and Algae Research
Type
article
Field-Weighted Citation Impact
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article

Immobilization of Enzymes Using Water-Soluble Metal-Organic Polyhedra

Benjamin Le Ouay, Masaaki Ohba
Kobunshi
Diatoms and Algae Research
article

Immobilization of Enzymes Using Water-Soluble Metal-Organic Polyhedra

Benjamin Le Ouay, Masaaki Ohba
article en

Abstract

Immobilization of enzymes is a potent strategy to improve their applicability for industrial or technological applications. This highlight describes our strategy of developing a family of cage-like compounds called metal-organic polyhedra (MOPs) functionalized to have a high solubility in water, in order to form self-assembled structures with enzymes. The high affinity of the developed MOPs for the surface of proteins enabled an easy yet versatile “Mix-and-shake” method to form aggregates in which enzymes are cross-linked by robust microporous units. Furthermore, the physical state of the MOP-enzymes composites, from colloids to solid precipitates, can easily be controlled by adjusting the mixing MOP-to-protein ratio. Immobilized enzymes maintained a high catalytic activity in the solid-state, and also showed a good recyclability and an improved stability. Furthermore, the unique nature of MOPs as well-defined yet highly tunable nanosized molecular entities can be used to mimic microscale environments in complex systems, and modify proteins’ configuration and activity in well-controlled conditions.

KobunshiVol. 74(1)
Kyushu University (JP)
Clean water and sanitation
Openalex Percentile: Top 88%
Diatoms and Algae Research
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