Novel interface-binding chloroperoxidase for interfacial epoxidation of styrene

Area of Science:

• Biocatalysis
• Enzyme Engineering
• Materials Science

Background:

• Chloroperoxidase (CPO) is a versatile enzyme with potential in industrial applications.
• Native CPO in aqueous solutions faces limitations in catalytic efficiency and stability.
• Interfacial biocatalysis offers a promising strategy to overcome these limitations.

Purpose of the Study:

• To develop an interface-binding CPO for enhanced biocatalysis.
• To investigate the impact of self-assembly at oil-water interfaces on CPO's catalytic performance.
• To evaluate the stability and side-reaction suppression of the modified enzyme.

Main Methods:

• Conjugation of native CPO with polystyrene (PS) to create a surfactant-like structure (PS-CPO).
• Self-assembly of PS-CPO at oil-water interfaces.
• Assessing catalytic efficiency and productivity for styrene epoxidation under batch and continuous feeding conditions.
• Evaluating enzyme stability and side-reaction profiles.

Main Results:

• PS-CPO self-assembled effectively at oil-water interfaces, maintaining enzyme enantioselectivity.
• A 2.5-fold enhancement in enzyme productivity was observed for PS-CPO versus native CPO in batch reactions.
• A remarkable 25-fold improvement in productivity was achieved in continuous feeding reactions, reaching 10 micromol h-1 mg protein-1.
• PS-CPO demonstrated suppressed side reactions (e.g., hydrolysis) and enhanced enzyme stability.

Conclusions:

• Interface-binding CPO (PS-CPO) significantly improves catalytic efficiency and productivity.
• Enzymatic self-assembly at interfaces offers a robust strategy for enzyme immobilization and performance enhancement.
• PS-CPO exhibits superior stability and reduced side reactions, making it suitable for industrial biocatalysis.