Catalase-only nanoparticles prepared by shear alone: Characteristics, activity and stability evaluation

Area of Science:

• Biotechnology
• Enzyme Engineering
• Nanotechnology

Background:

• Therapeutic enzymes like catalase face inactivation and degradation challenges in bioprocesses and in vivo delivery.
• Stabilizing enzymes is crucial for their effective application in pharmaceuticals and biotechnology.

Purpose of the Study:

• To develop a method for creating stable catalase-only nanoparticles using shear stress.
• To evaluate the conformational changes, activity, and stability of these nanoparticles compared to native catalase.

Main Methods:

• Catalase-only nanoparticles were prepared using shear stress in a coaxial cylinder flow cell.
• Nanoparticle properties (size, polydispersity, zeta potential) were characterized.
• Conformational changes were analyzed using spectroscopy; enzyme activity and stability were tested under various conditions (storage, simulated intestinal fluid with proteases).

Main Results:

• Shear-induced conformational changes in catalase were minimal compared to desolvation methods.
• Catalase nanoparticles retained over 90% of initial activity and showed significantly improved storage stability.
• Nanoparticles exhibited enhanced resistance to protease degradation in simulated intestinal fluid.

Conclusions:

• Catalase-only nanoparticles prepared by shear stress offer superior stability and activity retention.
• This method provides a promising approach for stabilizing enzymes for pharmaceutical and bioprocess applications.
• Enzyme nanogranulation enhances protease resistance, crucial for in vivo therapeutic use.