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Engineering enzyme conformation within liquid-solid hybrid microreactors for enhanced continuous-flow biocatalysis.
Xiaoting Hao1,2,3, Shuo Wang1, Xiaoming Zhang4,5
1School of Chemistry and Chemical Engineering, Shanxi University, Taiyuan, 030006, China.
Nature Communications
|November 30, 2024
Summary
Engineered enzymes in a novel microreactor system show significantly enhanced activity and stability for industrial biocatalysis. This approach improves enzyme performance in continuous-flow processes, paving the way for practical applications.
Area of Science:
- Biotechnology
- Enzyme Engineering
- Chemical Engineering
Background:
- Enzyme engineering for industrial applications requires enhanced catalytic activity and stability outside cellular environments.
- Continuous-flow biocatalysis offers advantages for industrial processes but faces challenges in enzyme stability and performance.
- Ionic liquids (ILs) and microreactors are explored for enzyme immobilization and process optimization.
Purpose of the Study:
- To develop a novel strategy for enhancing enzyme performance in continuous-flow biocatalysis.
- To investigate the combined effect of a hybrid microreactor and a functionalized ionic liquid on enzyme configuration, activity, and stability.
- To correlate enzyme conformational changes with altered enzymatic properties.
Main Methods:
- Design and implementation of a liquid-solid hybrid microreactor.
- Development of a polyethylene glycol functional ionic liquid (PEG-IL) microenvironment for enzyme encapsulation.
- Enzyme kinetic resolution using a model lipase system.
- Experimental characterization of enzyme activity, stability, and conformational changes.
- Molecular dynamics simulations to elucidate stabilization mechanisms.
Main Results:
- The PEG-IL microenvironment within the hybrid microreactor resulted in a 2.70 to 30.35-fold increase in lipase activity compared to batch or traditional IL methods.
- Encapsulated lipase exhibited significantly enhanced thermal stability, maintaining activity for up to 1000 hours at 60°C in a continuous-flow setup.
- Molecular dynamics simulations revealed that PEG groups stabilize enzyme secondary structures by delaying unfolding at elevated temperatures, correlating with improved enzymatic properties.
Conclusions:
- The developed hybrid microreactor system with PEG-IL effectively controls enzyme configuration, leading to superior activity and stability.
- This approach offers a promising strategy for designing high-performance enzymatic systems for real-world biocatalysis.
- The findings provide guidance for advancing industrial biotechnology through enzyme engineering and process optimization.
