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Evaluating the Performance of Different Substrates for Preparing Enzyme-Immobilized Bioreactors
Mahbuba Jannat1, Swarnila Chakma1, Md Junayed1
1Department of Chemical Engineering, Bangladesh University of Engineering and Technology, Dhaka-1000, Bangladesh.
ACS Omega
|December 1, 2025
Summary
Glass slides offer superior stability and reusability for immobilizing horseradish peroxidase (HRP) enzymes in bioreactors compared to silicone tubing, making them ideal for phenol degradation applications.
Area of Science:
- Biotechnology
- Enzyme Immobilization
- Bioreactor Design
Background:
- Enzyme immobilization requires stable and reusable substrates for efficient enzymatic bioreactors.
- Horseradish peroxidase (HRP) is a key enzyme for various biocatalytic applications, including pollutant degradation.
Purpose of the Study:
- To evaluate glass slides and silicone tubing as substrates for HRP immobilization.
- To compare the stability, reusability, and storage of HRP-immobilized bioreactors on different substrates.
Main Methods:
- Substrate treatment with (3-amino-propyl)-triethoxy-silane (APTES), followed by dextran polyaldehyde (DPA) or glutar-aldehyde (GA).
- Immobilization of HRP onto treated glass slides and silicone tubing.
- Phenol degradation assays to determine enzyme activity, loading, reusability, and storage stability.
Main Results:
- HRP immobilized on glass slides degraded 21% phenol, while silicone tubing degraded 10%.
- DPA-treated glass slides showed maximum HRP loading (6%) and activity (2.52 U).
- Glass slide bioreactors maintained 100% activity after 8 cycles and 4 months of storage, while silicone tubing retained 91.5% activity after 8 cycles and 90% after 4 months (GA-treated).
Conclusions:
- Glass slides, particularly DPA-treated ones, are superior substrates for HRP immobilization due to enhanced stability and reusability.
- DPA-terminated glass slides offer excellent ready-to-use substrate potential for HRP-immobilized bioreactors.
- The choice of substrate significantly impacts the performance and longevity of enzyme immobilization in bioreactor applications.
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