[Development of enzyme immobilization systems for CO₂ bioconversion: advances and challenges]

Area of Science:

• Biocatalysis
• Green Chemistry
• Materials Science

Background:

• Enzyme-catalyzed carbon dioxide (CO2) reduction offers a sustainable route to valuable chemicals, addressing environmental concerns and energy demands.
• Formate dehydrogenase (FDH) and multi-enzyme systems are key for converting CO2 into high-energy density products like formic acid and methanol.
• Limitations in enzyme activity, stability, and reusability hinder the industrial application of CO2 reduction processes.

Approach:

• This review explores enzyme immobilization strategies using diverse carriers, including membranes, inorganic materials, metal-organic frameworks (MOFs), and covalent organic frameworks (COFs).
• It details various immobilization techniques and evaluates the advantages of different carrier materials.
• The integration of immobilized enzymes with electrocatalytic and photocatalytic systems for enhanced CO2 reduction is also examined.

Key Points:

• Enzyme immobilization significantly improves enzyme performance, overcoming challenges related to activity, stability, and reusability.
• Advanced materials like MOFs and COFs offer promising platforms for efficient enzyme immobilization.
• Synergistic effects in coupled systems, combining immobilized enzymes with electrocatalysis or photocatalysis, boost CO2 conversion efficiency.

Conclusions:

• Enzyme immobilization is a critical technology for advancing CO2 utilization.
• Integrated catalytic systems show great potential for efficient and sustainable CO2 valorization.
• Further research into enzyme immobilization and coupled reaction systems is needed to address current challenges and unlock future development prospects.